Education

November 2014: Colliding worlds

Royal Society R.Science - 1 December, 2014 - 10:17

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Categories: Education

Practised procrastination

Chemistry World blog (RSC) - 27 November, 2014 - 18:01

Guest post by Heather Cassell

It’s an inevitability – there’s a task that should be doing but you can’t build up the enthusiasm. Normally mundane jobs can suddenly seem much more interesting to do.

A suspiciously tidy lab bench
Image by Jean-Pierre from Cosne-Cours-sur-Loire, France CC-BY-SA

For me it is always report writing. Although I love putting all of my results into order and writing it up succinctly for my colleagues and collaborators, I find I can rapidly lose focus. This is when the procrastination sets in. It never seems to matter how near the deadline is, how interesting my results are, or how important the document is – I feel an overwhelming desire to tidy my desk. ‘It’s important,’ I tell myself, ‘because if my desk is tidy I’ll have easy access to the papers and results I need to finish my report’. Just as a teenager’s room is never tidier than exam time, a researcher’s desk might only ever be clear when there’s a report to write.

Oh, but there are so many temptations! I’ve learned that when I’m meant to be writing a report it is best if I avoid the internet (see my previous post on the things you can discover while trawling twitter), so to physically remove the temptation often I’ll head into the lab.

But even the lab is full of potential distractions and procrastinatory aids, as there are always a diverse range of things to do! There is that pile of tip boxes that need refilling (it may have been gathering dust for weeks, but it seems urgent that they are to be filled and taken to autoclave). There are the consumables that need restocking, the buffers that need to be made, and stock solutions that need to be prepared. To the procrastinating mind, they all become more important than the task in hand. ‘If I’m not organised in the lab,’ I justify to myself, ‘then how can I work efficiently when I have finished my report?’

I try to reason with myself. I set targets and deadlines, promising myself a break if I can just reach the end of this section. As with exam dates and revision, eventually the deadline becomes so pressing that the level of stress rises and I actually buckle down to get on with the report.

It feels so good when it’s done that I consistently make promises to myself: ‘next time it will be different’; ‘next time I’ll just get it done without the distractions’. But the urge to procrastinate always returns. Who knows, without that urge my desk may never be clear.

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Categories: Education

Countdown to the 2014 Chemistry World science communication competition

Chemistry World blog (RSC) - 21 November, 2014 - 11:05

In this first of a series of guest posts, Elizabeth Tasker writes about the how and why of her piece on cosmic chemistry, which was shortlisted in the 2013 Chemistry World science communication competition.

Elizabeth TaskerThere are some stories that beg to be written. When you find an experimental astrophysicist building a star-forming cloud in his laboratory, there is practically a moral obligation to remind the world that there are no boxes for ideas.

Astrophysicists usually come in three flavours: observers (telescope kids), theorists (‘The Matrix’ universes) and instrument builders (hand me a hammer). We cannot typically perform laboratory experiments since putting a star (or planet or black hole) on a workbench is distinctly problematic. The closest we come to hands-on experiments is through computer models, which is the toolkit I use when studying the formation of star-forming clouds. However, Naoki Watanabe had gone ahead and built his own cloud  in a super-cooled vacuum chamber.

What I liked most about Naoki’s work was the science question that was the heart of his project. Rather than take the tools of a given discipline and ask what could be learned, Naoki had picked the question and then drew knowledge he needed from astronomy, atomic physics and chemistry. This mingling of traditionally discrete subjects also made it a great fit for Chemistry World’s 2013 science communication competition theme of ‘openness’.

Discovering I’d been shortlisted was amazing. This feeling was briefly replaced by terror, since I was asked to produce a video clip describing my article as I was unable to attend the prize ceremony itself.

I recorded and re-recorded the video 10 times. All of them were identical. I feel there is a lesson to be learned about perfectionism that I likely failed to entirely grasp.

It was great to know that the judges had both enjoyed my article and were as excited as me about interdisciplinary work. Perhaps it is time to stop calling myself an ‘astrophysicist’ and simply say ‘scientist’.

Elizabeth Tasker is an assistant professor in astrophysics at Hokkaido University in Japan, where she explores star formation though computational modeling. Originally from the UK, Elizabeth completed her MSci in theoretical physics at Durham University, before pursuing her doctorate at the University of Oxford. Elizabeth keeps her own blog. She is working on a book on exoplanets (The planet factory), which will be published in 2016.

 

If you are passionate about science and science communication, the 2014 Chemistry World science communication competition on the topic of chemistry and art offers a fantastic opportunity to demonstrate your skill, win £500 and be published in Chemistry World.

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Categories: Education

From Mould to Medicine

Chemistry World blog (RSC) - 20 November, 2014 - 10:29

Guest post by Rowena Fletcher-Wood

Excited, Mary Hunt tipped out the produce of her shopping: a large moulded cantaloupe. She had come across the cantaloupe by chance, and the ‘pretty, golden mould’ had proved irresistible. She had discovered the Penicillium chrysogeum fungus, a species that turned out to produce 200 times the volume of penicillin as Fleming’s variety. It was a serendipitous discovery, and vital at a time when the greatest challenge facing medicine was producing enough of the antibiotic to treat all of the people who needed it.

Hunt’s finding has been barely noticed beside the original accidental discovery: Fleming’s return from holiday to find a ‘fluffy white mass’ on one of his staphylococcus culture petri dishes. Fleming was often scorned as a careless lab technician, so perhaps the contamination of one of his dishes – which had been balanced in a teetering microbial tower in order to free up bench space – was not that unexpected. But Fleming had the presence of mind to not simply dispose of the petri dish, but to first stick it beneath a microscope, where he observed how the mould inhibited the staphylococcus bacteria. Competition between bacteria and fungi was well known and, in fact, when Fleming published in the British Journal of Experimental Pathology in June 1929, the potential medical applications of penicillin were only speculative.

In 1897, a 23 year old French scientist, Ernest Duchesne, published his doctoral thesis on antagonism between moulds and microbes – specifically, Penicillium glaucum versus Escherichia coli. His insight into the healing power of penicillin extended as far as curing guinea pigs of typhoid, but his research was never recognised.

Fleming lacked the resources and chemical training to isolate and test the active ingredient in penicillin, so he handed his research over to pathologist Howard Florey in 1938. Florey quickly transformed his Oxford lab into a penicillin factory. However, even with the discovery of Penicillium chrysogeum, production was slow.

The first patients to formally trial penicillin were a cluster of 25 streptococcus-infected mice. Unlike their 25 less fortunate friends who were not given the new medicine, they made a full and swift recovery. In 1940, Oxford policeman Albert Alexander became the first human to take penicillin. Alexander was suffering from fatal septicaemia, but within 5 days of treatment he began to recover. Sadly, the penicillin ran out and as techniques at the time were unable to produce enough, Alexander died. Although it was widely administered amongst the troops during World War II, once again, production was limiting.

The real breakthroughs in penicillin production began shortly after the establishment of a new American lab; in particular, the casual introduction of corn-steep liquor, a by-product of the corn wet milling process. This was being mixed with a wide variety of substances in an effort to find a use for it, and was seen to significantly increase penicillin yields.

In 1942, Anne Miller, suffering blood poisoning after a miscarriage, became the first successful civilian recipient, but further tests were still needed to explore the range of diseases treatable by penicillin.

Horrifically, in 1946-8, the Public Health Service, Guatemalan government, National Institutes of Health and the Pan American Health Sanitary Bureau approved a study to infect prison inmates, asylum patients, and Guatemalan soldiers with STDs and treat them with penicillin. Over 1300 people were infected, and 83 died.

Today, penicillin is the most used antibiotic in the world, treating large numbers of dangerous diseases. It also has many derivatives, the discovery of which began in 1957, when John Sheehan developed the first total synthesis. Although the synthesis proved difficult to upscale, it nevertheless produced a 6-aminopenicillanic acid intermediate – the starting material for a whole new class of antibiotics. Although the penicillin you and I take is manufactured in a lab, the battle between fungi and bacteria continues, and you can still come across this world-changing substance naturally growing in its parent mould.

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Categories: Education

Take 1… minute for chemistry in health

Chemistry World blog (RSC) - 17 November, 2014 - 10:00

Guest post by Isobel Hogg, Royal Society of Chemistry

Can you explain the importance of chemistry to human health in just one minute? If you’re an early-career researcher who is up to the challenge, making a one  minute video could win you £500.

The chemical sciences will be fundamental in helping us meet the healthcare challenges of the future, and we at the Royal Society of Chemistry are committed to ensuring that they contribute to their full potential. As part of our work in this area, we are inviting undergraduate and PhD students, post-docs and those starting out their career in industry to produce an original video that demonstrates the importance of chemistry in health.

We are looking for imaginative ways of showcasing how chemistry helps us address healthcare challenges. Your video should be no longer than one minute, and you can use any approach you like.

The winner will receive a £500 cash prize, with a £250 prize for second place and £150 prize for third place up for grabs too.

Stuck for inspiration? Last year’s winning video is a good place to start. John Gleeson’s video was selected based on the effective use of language, dynamic style, creativity and its accurate content.

The closing date for entries to be submitted is 30 January 2015. Our judging panel will select the top five videos. We will then publish the shortlisted videos online and open the judging to the public to determine the winner and the runners up.

For more details on how to enter the competition and who is eligible, join us at the Take 1… page.

Good luck!

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Categories: Education

How to win a Nobel Prize, cover by cover

Chemistry World blog (RSC) - 13 November, 2014 - 05:15

Guest post from Tom Branson

Last month’s Nobel prizes gave the world some new chemical heroes, but have also given me an opportunity to delve into the art of how to become a winner. Eric Betzig, Stefan Hell and William Moerner shared the prize in chemistry for ‘the development of super-resolved fluorescence microscopy’, which sounds, and indeed is, a very photogenic area of chemistry.

Through my exhaustive research of the prize winners’ websites, I found a handy list of journal covers on the Moerner group site. The other prize winners show off impressive lists of publications, but no helpful collection of cover art for me to plunder. So my apologies to Betzig and Hell: you may have Nobel prizes, but that doesn’t quite cut it here. Instead, let’s concentrate on Moerner and see what journal cover art can teach us about becoming a champion of science.

Moerner’s website shows nine journal covers, although it is not clear if this is an exhaustive list of the group’s artistic career. From this list, we can see that Moerner has a rough average of one journal cover per 38 articles published. Just for comparison, I’ve published a whopping three articles and had one featured on a journal cover, a much better conversion rate than Moerner. So does this totally non-scientific analysis suggest that I might be a dark horse for next year’s prize?

The most recent cover shown on Moerner’s website is from an article published last year in Nano Letters. A rather powerful magnifying glass is shown looking down at some fluorescing molecules and a large shaking arrow. A simple image that illustrates the crux of the work very nicely. There is more to see here than just pretty colours: the paper stresses the importance of analysing the oscillating behaviour of the molecules in order to achieve the best resolution with your magnifying glass microscope.

Another image from the Moerner group made it to the front of Nature Chemistry in 2010. Now this one, I really like. A pile of film rolls is shown with proteins captured in a new position on each frame, firing off bright reds and yellows. This is pretty much exactly what actually happens in the experiments. The camera-friendly proteins are very elegantly portrayed here on old Kodak film roll, probably because this is somewhat easier to imagine and more iconic than the digital storage relied upon in today’s techniques. The specific protein shown is allophycocyanin, a photosynthetic antenna protein that the group tracked, monitoring changes in florescence by using an anti-Brownian electrokinetic trap.

That same issue of Nature Chemistry features an editorial all about cover art. The editorial gave some tips as to what makes an attractive image and are open enough to admit that what really matters ‘is that you impress the editorial and production teams, who all get to have their say – and, in particular, the art editor.’ So just like the Nobel prizes themselves, where everyone has their own opinion, what counts in the end is to impress the judges.

The Nature Chemistry masterpiece wasn’t Moerner’s first high impact cover. Research from his group featured on the front of Science back in 1999 where some less-than-groundbreaking graphics, were used to highlight some definitely-groundbreaking research. His work has also featured on the covers of Nature Structural Biology and the Biophysical journal.

As for my own Nobel prize aspirations, I should aim to see my work on the front of a few more journals, for which I think I’ll need to publish a few more articles. I also assume the Nobel selection committee are not as easily dazzled by pretty pictures as I am. The road to Nobel prizedom may not be paved with covers, but showing off your artwork surely helps along the way.

If you come across some cover art that you believe to be prize winning material, or are simply seeking shameless self-promotion, then please get in touch with me in the comments or on Twitter (@TRBranson).

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Categories: Education

Academic Family – Dorothy Hodgkin

Chemistry World blog (RSC) - 6 November, 2014 - 10:10

Guest post by JessTheChemist

A few months ago I wrote a blog post about the first British Nobel prize winner, Sir William Ramsay, so I thought it was about time that I wrote about Britain’s first (and only) female winner of the Nobel prize in chemistry, Dorothy Crowfoot Hodgkin. I first heard about Dorothy Hodgkin while I was studying at Durham University, through my ex-head of department and an amazing lecturer, Judith Howard. My most vivid memory of her is a second year lecture where she taught us about space groups using balloons, sticks and potatoes. As a postgraduate student in Dorothy Hodgkin’s lab, she carried out postgraduate research on neutron diffraction (mostly under the supervision of Terry Willis from the UK Atomic Energy Authority).

Dorothy Hodgkin was an inspiring woman. She broke boundaries in many ways, not least by joining in the boys’ chemistry lessons at school. Through help from her auntie, she was able to attend university and developed a passion for biochemistry. She completed postgraduate studies on x-ray crystallography at the University of Cambridge under the supervision of John Bernal. Bernal was, himself, an interesting and controversial scientist. During World War II, he rescued Max Perutz from internment, getting him to perform experiments in a meat store freezer below Smithfield Meat Market.1 Pertuz also won the Nobel prize for chemistry for studies of the structures of haemoglobin and myoglobin in 1962.

After her postgraduate studies, Hodgkin moved to the University of Oxford, where her research focussed on protein crystallography. During this time, she became acquainted with James Watson, Francis Crick and Rosalind Franklin, and as a result, she was one of the first people invited to see the model of the double helix structure of DNA. Her research achievements are many but include the confirmation of the structures of penicillin and vitamin B12 and it was for these achievements that she won the Nobel prize in chemistry in 1964 for ‘her determinations by X-ray techniques of the structures of important biochemical substances’.

Apart from Judith Howard, Dorothy Hodgkin had other famous female academic descendants. Of particular note is Margaret Thatcher, who was a student in her Oxford lab in the 1940s. Of course, Thatcher famously went on to be Britain’s first (and so far only) female Prime Minister and not a scientist. There are many other famous scientists in Hodgkin’s family tree. Through Bernal, Hodgkin is connected to famous father and son duo, Sir William H. Bragg and Sir W. Lawrence Bragg ,who shared the Nobel prize in physics in 1915 ‘for their services in the analysis of crystal structure by means of x-rays. As an alumnus of the University of Leeds, I was excited to discover that William H. Bragg was Cavendish chair of physics there. Further links to the University of Leeds can be found through John Bernal, who is connected to William Astbury, a former chair in biomolecular structure at Leeds, who pioneered x-ray diffraction studies of biological molecules.

As you can see, Dorothy Hodgkin is connected to a large number of influential scientists, both male and female. What is most striking about this particular academic family tree is that it is based around Britain’s only female Nobel prize winner in chemistry. This was awarded 50 years ago, and I think it’s about time we added to that tally. So come on ladies, get researching!

 

Reference:

1: J. D. Bernal: The Sage of Science. Andrew Brown, Oxford University Press, 2005

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Categories: Education

October 2014: The Royal Society at the Party conferences

Royal Society R.Science - 3 November, 2014 - 13:05

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Sleep deprivation and science

Chemistry World blog (RSC) - 30 October, 2014 - 11:30

Guest post by Heather Cassell

This blog post is inspired by my 3 month old and 6 year old who are both suffering from a cold and not letting me get much sleep.

Over the years I have found sleep deprivation can have a significant impact on my work in the lab. There are many ways to end up overly tired: a child could be keeping you awake, you may be unlucky enough to have insomnia, or you might have been up late doing something much more fun (in which case you get less sympathy). The sensible approach would be to take some time and get some sleep, knowing you will be more productive tomorrow. But often you simply don’t have that luxury, as there is important science to be done.

Sleeping on the job – not a good idea in the lab
©iStock

Sleep deprivation often hits at the least opportune moment, when you most need the sleep. It’s often a deadline that you really need to get results for – be it a conference, a report, or a meeting with your collaborators. ‘If only I can get these experiments finished then my data will be much more convincing! (As long as they agree with the previous results)’. When you have an experiment to do that needs careful set up, has a complicated protocol to follow and many time points to take, or takes many days to run, luck will have it that you will be sleep deprived at the crucial moment.

In situations like this you need to carefully consider what to do – start the experiment now and risk mistakes, or postpone it until you’re less dozy and miss out on the data? If you decide to work through the tiredness, then I recommend you make a detailed, foolproof plan. This will ensure that you don’t need to think, just to do. Also, drink as much tea as you dare before you head to the lab to get started – you’ll need to find your own balance of under-caffeinated versus excessive toilet trips. At times like this, I’m tempted to smuggle a cup of tea into the lab, just to help get through the day.

I’m not proud to say that I have reached the point where I’m so sleep deprived that I go into denial – I believe that I can work normally on a small amount of sleep – and that is when the serious mistakes creep in. My tales of woe include throwing away a solution containing the protein that I had spent two days purifying; or using the wrong antibiotic, and so preventing the growth of my cells. It may have reached my nadir when I only put labels on the lids of a stack of 96 well plates: I put them to one side while adding something to the plates, only to realise that I could no longer tell one plate from another. Analysis of the results was impossible; I had wasted time and resources, all because I refused to acknowledge my limits.

These slip-ups are frustrations, but other mistakes could potentially be much more serious. There are hazards in a lab that we are all trained to understand and risks that we’re equipped with the tools to mitigate. Safe lab work requires each of us to be fully conscious – if we fail to assess risks properly because we’re tired, we put far more than some experimental data at risk. A lab full of zombie-like sleepwalking scientists is not a safe lab to work in.

Every time I’ve made one of these mistakes, I’ve realised that it’s time to get out of the lab and do something else, maybe write up my lab book, skim a few journals or make another cup of tea. But sometimes an extra hour in bed is justified – the results can wait until another day.

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Categories: Education

ISACS winners 2014

Chemistry World blog (RSC) - 24 October, 2014 - 11:11

Congratulations to all of our ISACS Chemistry World poster prize winners this year. Here’s a run-down of the winners:

Katie-Louise Finney receiving her prize from Chemistry World features editor, Neil Withers

Katie-Louise Finney, a second year PhD student in David Parker’s group at the University of Durham, UK, was the winner at ISACS 13 (Challenges in Inorganic and Materials Chemistry), held in Dublin, Ireland. Katie’s poster was titled ‘Development of 1H PARASHIFT probes for magnetic resonance spectroscopy and imaging‘.

Katie explains her work: ‘Our 1H PARASHIFT probes possess a tert-butyl reporter group that can be shifted well away from the water and fat signals at 4.7 and 1.3ppm. We have succeeded in shifting the tert-butyl reporter group as far as +65 and –75ppm. This means that in imaging experiments, we gain two orders of magnitude of sensitivity due to 1) the lack of background signal in vivo and 2) the enhanced reporter group relaxation by the proximal lanthanide ion. As a result, our probes have been imaged in live mice within minutes, at concentrations of 0.1mmol/kg.’

We’ve actually featured Katie’s MRI work in Chemistry World before in our article Moving the goalposts for MRI.

Baihua Ye

Baihua Ye, a doctoral assistant in the laboratory of asymmetric catalysis and synthesis at the Swiss Federal Institute of Technology in Lausanne, was the winner at ISACS 14 (Challenges in Organic Chemistry), held in Shanghai, China.

Baihua’s poster was titled ‘Development of chiral cyclopentadienyl ligands for Rh(III)-catalysed asymmetric C-H functionalisations‘.

Baihua explains his poster: ‘My PhD thesis under the supervision of Nicolai Cramer was devoted to the investigation of novel cyclopentadienyl (Cp) ligand as a stepping stone for the asymmetric rhodium(III)-catalyzed C-H functionalizations. The challenge to achieve the high level of enantioselectivity basically stems from the spatial arrangement of the three coordinating components around the metal center. The Cp derivative, thus, acts as the sole source of chirality. From the year of 2012, we have pioneered on the design of chiral Cp ligands and elaborated two complementary families of the CpRh(I) complexes. Upon the facile oxidation in situ of the Rh(I) species, the resulting chiral CpRh(III) have been successfully applied in the C-H functionalizations of aryl hydroxamates coupled with olefins, allenes as well as diazo esters. The corresponding heterocyclic products are generally obtained in good yields with high levels of regio- and stereo-selectivity. In the future, we believe that our effort would provide more variant on enantioselective Cp-based metal catalysis.’

David Ordinario

David Ordinario, a graduate research assistant in Alon Gorodetsky’s group at the University of California at Irvine, was the winner at ISACS 15 (Challenges in Nanoscience), held in San Diego, US. David’s poster was titled ‘Protonic devices from a cephalopod structural protein‘.

David explains his poster: ‘In my poster, I first introduced the reflectin protein, explained where it comes from, and described some of its unusual but interesting properties. Next, I explained our electrical characterisation work on thin films from the reflectin protein. We performed tests such as two- and three-terminal IV measurements and electrochemical impedance spectroscopy (EIS). Finally, I showed and explained the protonic transistor devices we fabricated which uses reflectin as the active material. I focused on explaining the underlying mechanisms by which the reflectin-based protonic transistors function, as well as a couple of methods we developed to optimise the performance of the transistors.’

The next ISACS, ISACS 16: Challenges in Chemical Biology, will held be in Zurich, Switzerland, from 15–18 June 2014. See the Royal Society of Chemistry’s ISACS 16 event page for details.

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Categories: Education

The Devil’s Element

Chemistry World blog (RSC) - 23 October, 2014 - 16:05

Guest post by Rowena Fletcher-Wood

‘The Alchymist, in Search of the Philosopher’s Stone, Discovers Phosphorus, and prays for the successful Conclusion of his operation, as was the custom of the Ancient Chymical Astrologers’ – Joseph Wright of Derby

Hennig Brand was known as ‘the last of the alchemists’, even though Isaac Newton, possibly the most famous alchemist, outlived him by between 17 and 35 years. This number is vague for a reason: strangely enough for a man who spent his time searching for eternal life, there is no record of when or how Brand died. Like his alchemy, he appears to have disappeared into a puff of mysticism.

Although alchemy had been around since at least 500BC, it had never had any luck with its most famous quests: transmutation of metals and the hunt for the elixir of life, both thought to be capacities of the mysterious philosopher’s stone. A secretive practice, (alchemists often wrote their recipes in arcane code) it seems ironic that its last legacy was illumination: the unnatural glow of a strange, white, waxy and translucent material, the first element to be chemically discovered, and the 13th known to man. It was called the Devil’s element. And its method of discovery in 1669 is certainly something best reserved for horror stories. Brand wasn’t trying to make the luminous substance he originally dubbed ‘cold fire’, of course: he was trying to turn lead into gold.

Using valuable techniques later appropriated into modern science, he followed a procedure typical of alchemy. This involved boiling, filtering and purifying as many as 60 buckets of bodily fluids in attempts to understand the ‘essence’ of living things. His fluid of choice was urine, which he allowed to rot for several days until it became powerfully pungent. Just as the smell became unbearable, Brand distilled his urine down to a black paste and left it to fester for months. Later, he heated it with sand to vaporise off the oily components, which he trapped and condensed with water to give the material he hoped was gold.

It wasn’t. But it did have some unusual properties. It glowed an eerie green in the dark but, left in a stoppered jar, eventually extinguished. In open air, it would ignite spontaneously, producing acrid flames and a brilliant light; under vacuum, it sublimed to a gas upon light exposure. It melted at just 44°C and was highly toxic, burning skin upon contact. Brand had accidentally discovered white phosphorus, and two other allotropic forms, red and black, would later be identified.

The name phosphorus derives from phosphoros mirabilis – ‘miraculous bearer of light’.

Always a good alchemist, Brand originally tried to keep his discovery a secret, although he readily gave away his supplies of phosphorus. He finally sold the secret of his synthesis to three alchemists, including Johann Daniel Kraft, who toured much of Europe with it. The secret escaped – first it leaked from Johann Kunckel in Sweden, and two years later from Robert Boyle in England, who had met with Kraft during his travels and heard how phosphorus was derived from ‘somewhat that belonged to the body of man’. Boyle followed the clues, synthesised and published on phosphorus (discovering meanwhile that the urine didn’t need to rot at all), and became the first person to use it to ignite sulfur-tipped wooden splints.

In later years, the ‘unnatural’ glow of phosphorus was explained by an excruciatingly slow surface reaction with oxygen, producing short-lived HPO and P2O2 emitters of visible light.

In the 1770s, Carl Wilhelm Scheele procured phosphorus from bone. Today, it is mostly prepared from calcium phosphate rock and used in the manufacture of phosphoric acid for fertilizers. It is also used for cleaning agents, water softeners, baking powder and fluorescent light bulbs. Red phosphorus is a starting material for safety matches, explosives, poisons and pyrotechnics. If you like, Brand’s alchemy has gone up in flames.

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Categories: Education

What can Sugru do for scientists?

Chemistry World blog (RSC) - 20 October, 2014 - 12:33

Looking around Form Form Form’s laboratory in Hackney, London, you can’t help but notice that the standard lab equipment has been modified, tweaked, personalised and adjusted using Sugru – the mouldable silicone rubber adhesive they manufacture. When I went to visit them with Phillip Broadwith, Chemistry World‘s business editor, to learn about the history and chemistry of Sugru, we asked a simple question: ‘what can Sugru do for scientists?’

Jude Pullen, head of R&D, took us through a handful of ‘lab hacks’ – quick and simple ways to make lab equipment safer, more efficient and easier to use:

Can you think of a way to use Sugru in the lab? Let us know by commenting below, or find us on Twitter: @ChemistryWorld

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Categories: Education

Is it a bird? Is it a plane? No, it’s Raney Cobalt-man!

Chemistry World blog (RSC) - 16 October, 2014 - 15:46

Guest post from Tom Branson

In a bold move by Organic and Biomolecular Chemistry, the journal has unveiled the latest superhero in the fight to save the common scientist from the ruthlessness of today’s laboratories.

With great power comes great selectivity

Standing firm with test tube in hand, Raney Cobalt-man is a new character from Catalyst Comics. The star wears a rather tight, bright cobalt blue coloured outfit, reflecting one of the element’s most notorious uses. How Raney Cobalt-man gained his powers, we will never know. But perhaps it was in a careless lab accident, and if so, he has certainly learnt his lesson. Now with goggles and elbow-length gloves (not to mention a full body suit and special groin area protection), Raney Cobalt-man is a true ambassador for PPE.

This first adventure takes our hero into the domain of the domino reaction where he’s be helped by his trusty sidekick, Dihydrogen Boy. The young assistant plays an essential role in their joint mission to catalyse peace and his support is needed even more as the hero ages. Here in the domino reaction, they join forces to selectively bring harmony cascading through the scientific community.

But where are the other great chemical heroes of today? Well, I suppose there is the elementally named Iron Man – a brilliant scientist, although he was actually more of an engineer. The Flash was first a forensic scientist who came by his powers after a lightning bolt hit his lab. This mishap is, of course, one of the many dangers of working alone late at night. The lovable Chemist Hulk may also be familiar to those folks on Twitter, this mean green scientist likes nothing better than to tweet about ‘SMASHING PUNY MOLECULES’.

Raney Cobalt-man is the hero that chemists deserve, but is it the one they need right now?

In this edition of the Raney Cobalt-man comics, the eponymous hero is helped by Martin Banwell and colleagues from the Australian National University. Together they review an underappreciated reagent and compare its powers to that of its nemesis, Raney Nickel-man. The story tells that high pressure from Dihydrogen Boy can often be off-putting for those wanting to call upon Raney Cobalt-man’s selective powers. But these drawbacks are simply overcome by using a larger amount of Raney Cobalt-man and therefore less of his annoying sidekick.

Comic book and science fans alike may be waiting a while before Raney Cobalt-man’s next adventure hits our book shelves, but be sure to pick up the first edition over at OBC.

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Categories: Education

With this ring…

Chemistry World blog (RSC) - 16 October, 2014 - 10:22

Guest post by Jen Dougan

I attended five weddings this year, between February and October, making 2014 most definitely the Year of the Wedding. Each day was unique and reflected closely the couple, their relationship, vision and hopes for the future.  And while there was a broad range of traditions at each, whether religious or humanist approaches, one tradition – the exchange of rings – provided a common element throughout.

The element is, of course, gold. But what is the chemistry of this symbol that is ritually shared as a sign of commitment and lasting love?

© Murray Robertson / Visual Elements

Gold is the most noble of metals, it doesn’t corrode or oxidise in the Earth’s moist, oxygen-rich atmosphere. Ductile and malleable, it can be fashioned at will and, since it doesn’t tarnish, is an ideal material for producing jewellery. The decorative attributes of gold have long been coveted – examples of gold jewellery have been found in the tombs of the Queens of Egypt and Sumeria, 3000 years BC.

Gold is one of only three coloured elemental metals (the others being copper and caesium). Most metals appear whitish-grey as they reflect all wavelengths of visible light. Gold, on the other hand, due to its electronic configuration exhibits a reduction in reflectivity efficiency in the blue region of the visible spectrum. It has, in the pure form, a striking yellow colour and brilliant lustre for which it became known by the latin Aurum, meaning ‘shining dawn’ (depicted by artist Murray Robertson in the image above).

Today the purity of gold jewellery is expressed in terms of ‘karat’. Pure gold is 24 karat, where, K = 24(Masspure/Masstotal), meaning 24/24 parts of the material are gold, by weight. In practice, even 24K gold is often stated as 99.99% pure due to residual impurities from the extraction process. Although 24K gold can be used for jewellery, the softness of pure gold means that alloying the metal to improve its physical properties or to design colour variants is a popular approach. The European standard, for instance, is 18 karat, meaning 18/24 parts are gold (75% pure by weight). The other 25 % of the weight is made up of another material (in the case of jewellery, a second metal) to make an alloy, which is typically stronger than the pure metal.

The improved strength of gold alloys occurs when, having melted two or more metals together, a new structural phase is formed on cooling. The precipitation of the added metal atoms reduces slippage of the original atoms across one another.

Ternary plot of approximate colours of Ag–Au–Cu alloys, which are commonly used in jewellery making.
Original image: Metallos [CC-BY-SA-3.0-2.5-2.0-1.0 (http://creativecommons.org/licenses/by-sa/3.0)], via Wikimedia Commons

Common alloys of gold for jewellery fall into the yellow gold or white gold categories. Most jewellery alloys of yellow gold, including that of rose and green-shade gold, fall within the Au-Ag-Cu system (see image above). Zn is sometimes added to further increase the alloy strength and to change the red colour of high Cu alloys to a paler rose.

For white gold, Au-Pd-Ag is a common alloy system, where Pd is used as a bleaching agent. Nickel, another metal capable of producing the desired bleaching effect to produce white gold, is a known skin sensitiser and has become less popular in jewellery making.

The bleaching effect occurs due to the added material changing the reflectivity of the alloy in the low energy part of the visible spectrum. In all cases, the relative ratio of the alloy’s components dictate the resulting hue and mechanical characteristics.  The alloy systems allow the characteristics to be achieved such that the design lasts the length of a marriage and beyond.

A word of warning/advice to the newlyweds: although your gold is stable, it is not chemically inert. Avoid exposure to mercury, with which the gold will form an amalgam; cyanide salts, which will react with your band; and aqua regia* in which it will dissolve. Of course, if you encounter any of these three materials by accident, you have greater worries than the integrity of your wedding ring!

The chemical susceptibility of gold for these reagents has proven useful. Mercury and cyanide salts have been used to extract gold from its ore. In fact, gold cyanidation, developed industrially in the 1880s by Glaswegian chemists John Stewart McArthur and Robert and William Forrest is still the main method of gold extraction – and the biggest use of sodium cyanide – globally. The ability of aqua regia to dissolve gold helped foil the Nazis during World War II. Two German Nobel laureates had placed their medals (23K gold) at the Niels Bohr Institute in Copenhagen for safe-keeping. But removing gold from Nazi Germany was a grievous offense and with the laureates names inscribed on the medal, this was an incriminating piece of evidence. ‘While the invading forces marched in the streets’, George de Hevesy – a (future) Nobel laureate himself – dissolved the medals in aqua regia. While the laboratories were laboriously searched by the Nazis, the medals remained dissolved, but undiscovered, on the bench. The metal was recovered after the war and the medals recast and returned to the laureates.

Whatever gold you choose for your wedding band, you add to a rich history of human civilisation fascinated by and adorned with gold. And to the newlywed class of 2014, congratulations!

 

 

* Note: Aqua regia is latin for ‘King’s water’, a 1:3 nitric:hydrochloric acid solution, it is known in Russia as Tsar’s vodka and its ability to dissolve gold is shown wonderfully in this Periodic Table of Videos.

References:

 

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Categories: Education

Academic family: the Nobel prize in Chemistry 2014

Chemistry World blog (RSC) - 14 October, 2014 - 13:29

Guest post by JessTheChemist

‘Where the telescope ends, the microscope begins. Which of the two has a grander view?’ – Victor Hugo

In 1873, German physicist Ernst Abbe reported that the resolution limit of the optical microscope was 0.2 micrometres. Although this still remains true, recent work in the field of microscopy – specifically Stimulated Emission Depletion (STED) microscopy and single-molecule microscopy – has allowed scientists to visualise molecules smaller than this limit. This is accomplished by tagging molecules with fluorescent labels, which allows a more detailed picture to be visualised. On Wednesday 8th October 2014 Eric Betzig, Stefan Hell and William Moerner were awarded the Nobel prize in chemistry for their ground-breaking work in ‘the development of super-resolved fluorescence microscopy’. You can learn more about the ins and outs of the Nobel prize winners’ work by reading the recent Chemistry World article.

I am interested in finding out how chemists are connected to each other, and in particular, investigating whether your likelihood of winning a Nobel prize is increased by having a high number of laureates in your family tree.  It is also interesting to see how closely related, if at all, are the scientists that share a prize.

If we consider his academic pedigree, one might say that Eric Betzig was destined to become a Nobel prize winner. He is connected to a number of notable laureates, including the father of nuclear physics, Ernest Rutherford. Rutherford won the Nobel prize for chemistry in 1908 ‘for his investigations into the disintegration of the elements, and the chemistry of radioactive substances’. Through Rutherford, Betzig is also connected to Niels Bohr, who won the Nobel prize for physics in 1922 for ‘his services in the investigation of the structure of atoms and of the radiation emanating from them’.

Additionally, Betzig is academically related to John William Strutt (Lord Rayleigh) who won the prize for physics for the discovery of argon in 1904, along with his collaborator Sir William Ramsay, who won the 1904 chemistry prize for the same discovery. With ancestry like that, Betzig was always destined for greatness.

Alternatively, William Moerner is closely linked to Dudley Herschbach and Yuan T. Lee, who won the 1986 Nobel prize in chemistry ‘for their contributions to the dynamics of chemical elementary processes’. To find out more about Herschbach and Lee’s academic family connections, check out last month’s blog post about one of their connections, Sir Harry Kroto.

Although Eric Betzig and William Moerner worked independently from one another, they both developed single-molecule microscopy, so it is not a surprise that their lineage is intertwined. As you can see from the tree, they are connected via some of the science greats such as Linus Pauling.

Stefan Hell worked in a slightly different field to Betzig and Moerner and, amongst others, is connected to biochemists Robert Huber and Johann Deisenhofer, who won the 1988 Nobel prize for chemistry ‘for the determination of the three-dimensional structure of a photosynthetic reaction centre’.  As predicted, however, all three of the prize winners can be connected through their academic relations – via Deisenhofer, Hell can be connected to Moerner and, therefore, Betzig.

As you can see, all three winners have a rich Nobel history but what I found particularly interesting about this academic family tree is that it contains scientists from all sorts of backgrounds – from nuclear physics to biochemistry to organic chemistry. This led me to think, what kind of scientists am I connected to? To find out what kind of scientists you are connected to, head to academictree.org, where you can add yourself to the website and start creating your very own tree.  You never know who you may be connected to.

And don’t forget to tweet me (@Jessthechemist) with suggestions for the focus of next month’s blog post!

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Categories: Education

September 2014: Newton, sun and ice

Royal Society R.Science - 6 October, 2014 - 15:56

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Categories: Education

Is someone drinking the solvents?

Chemistry World blog (RSC) - 2 October, 2014 - 14:46

Guest post by Heather Cassell

Space in the lab is always at a premium; you need more things than you have space for, so it makes sense for multi-group labs to share equipment, consumables and buffer stocks that everyone uses. This inevitably causes trouble when someone doesn’t look after the equipment, or fails to restock things after using them.

It is a frequent problem. You are about to start an experiment, so you’ve checked that the equipment will be free, you’ve planned your samples and now you just need to dilute from a communal buffer stock. All too often there is only a dribble left, so you have to make a fresh stock of buffer before you start, delaying your experiment by precious minutes. Your next stop is the communal chemical stocks, where you find there is either nothing left or such a trifling amount that it is of no use to anyone. This often prompts sarcastic mutterings of ‘how considerate’, or something rather more profane.

In my experience, this is especially common with flammable solvents. As these need to be kept in a special vented cupboard, there is only a limited amount of room for the big brown bottles they are delivered in. The nature of the bottles themselves also conspires to make it all too easy to get caught out: you check in advance that there is a bottle of solvent available, see one in the cupboard and relax into the next task. Of course, when you need it, the brown bottle has concealed the fact that there is only a drop left, never quite enough for what you need to do.

So how does a frustrated chemist deal with this situation? There are several options: you can go to the on-site chemical stores and buy a new one (assuming they are open and have what you need in stock); you can go begging to other groups to see if you can borrow some; or you can simply abandon your half made buffer or experiment and do something else instead.

Even for the renownedly polite English scientist, repeatedly buying a replacement bottle of the same solvent – even though you use only a small amount each time – can test the patience. You end up subtly enquiring to find out who else is using it, so you can politely suggest they stop leaving it in such a maddeningly useless state. Inevitably, your fellow lab denizens will only own up to using a small amount (never a large volume, oh no), and they always leave plenty in the bottle after use.

So where is the rest of the solvent going? As a scientist, I have to rule out untestable hypotheses like ‘the solution magically disappears’. I’ve also never seen a colleague drinking a cup of buffer (though it has occurred to me that they might), so either that isn’t the explanation or they’re very subtle about it. The answers to these questions may never found, but every time it happens you resolve to check more thoroughly before each planned experiment. Until the next time, of course…

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Categories: Education

Who will get the 2014 chemistry Nobel?

Chemistry World blog (RSC) - 30 September, 2014 - 14:10

With just under week until the announcements start, Nobel prize fever is officially here.

The official shortlist is shrouded in secrecy, giving those making their predictions about who might win little to go on – but that hasn’t stopped them.

— Nobel medal

As usual, Thomson Reuters have released their Nobel forecast, which uses citation numbers and other statistical wizardry to predict the winners in each category. This approach has successfully predicted 35 Nobel prize winners over the past 12 years.

This time round they highlight three possible chemistry winners – the inventors of the organic light emitting diode (Ching Tang and Steven Van Slyke), RAFT polymerization (Graeme Moad, Ezio Rizzardo, San Thang) and mesoporous materials (Charles Kresge, Ryong Ryoo, Galen Stucky).

Elsewhere, less official speculations – perhaps based more on a hunch – have begun flying around.  On the Everyday Scientist blog, chemist Sam Lord has put together some suggestions. Like the number crunchers at Reuters, Lord has some past successes (though he didn’t predict last year’s computational chemistry winners - Karplus, Levitt and Warshel). He thinks the 2014 prize could go to a key historical invention, such as the contraceptive pill, or the lithium-ion battery (also a top pick for The Curious Wavefunction blogger Ashutosh Jogalekar), but also mentions broader areas such as microfluidics, nanotechnology and next-generation sequencing. If last year is anything to go by, there’s much to be said for gut feeling as well as advanced number crunching. As always, we’ll just have to wait a little longer for that all-important announcement from Sweden.

If you want to get into the Nobel spirit and hear more about the possible winners this year, our features editor Neil Withers joined representatives from Nature Chemistry and C&EN to begin the countdown to the 2014 chemistry Nobel in a Google hangout – watch the whole discussion here.

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Categories: Education

Nylon – a bit of a stretch

Chemistry World blog (RSC) - 25 September, 2014 - 13:41

Guest post by Rowena Fletcher-Wood

I first heard the story of the discovery of nylon during a chemistry class in school – it was told as a serendipitous discovery. A young lab assistant, clearing up at the end of a long day, clumsily poured two mixtures in together and noticed a precipitate. Dipping in a stirring rod, he pulled out a thin string, which he stretched out into a tough, translucent fibre. He realised the potential of his discovery, reported it to his superiors and left them to the tiresome job of working out what he had done to make it.

The invention of nylon created a revolution in hosiery
©Shutterstock

It’s funny how we use accident to shape our understanding of discovery and achievement, as though we want to excuse hard work and apologise for years of learning. It’s somehow disappointing, unromantic: the story of research whisks away that tantalising fantasy of stumbling upon treasure, reserving discovery for the experts.

The real story of nylon, interesting though it may be, is a bit of stretch from serendipity.

There was a young lab assistant, and his name was Julian Hill. He was working in the DuPont research laboratory, led by the rigorous organic chemist Wallace Hume Carothers, who had taken on the challenging ‘synthetic fibre race’. At the time, synthetic polymers were a mysterious conception; what they were made of and how they related to simpler compounds was unknown. The DuPont team had studied complex natural products such as cellulose and silk and from their understanding had developed polyamides through the condensation of dicarboxylic acids with diamines – fantastically interesting but, at the time, not particularly useful.

Discovery of nylon, 1941 re-enactment. DuPont chemist Julian Hill (1904-1996) carrying out a re-enactment in 1941 of the discovery of nylon in 1935. A glass rod is being used to pull threads from the sample prepared in a glass tube. This discovery was made at DuPont’s Experimental Station near Wilmington, Delaware. Hill was a member of the team, along with other chemists. The molasses-like mass stuck to the glass stirring rod and was drawn out into a thin fibre. After more research and development, DuPont was able to commercialise the new material. Production started in 1939, twelve years after the research program had started in 1927. Credit: Hagley archive/Science Photo Library

Julian Hill had been working with polyester when, dipping in a stirring rod, he pulled out a thin string, which he stretched out into a tough, translucent fibre – just like in the story I was told. But this was not considered extraordinary. Often, discovery is not about observing properties, but recognising them. One day, when Carothers was absent from the lab, the chemists decided to go rogue with the polyester and have a competition to see how long they could stretch it. They raced down the hall, delicately extending the fibre. They had extended it to four times the original length when it stopped. It would not stretch any more.

Suddenly, Hill understood: as they stretched the fibre, chains of molecules snapped into position, orienting themselves into a chain of a discrete thickness. This would be the basis for the first fully synthetic fibres.

But nylon was far from invented. The melting points of the polyesters they had were far too low for any practical applications, and so they returned to polyamides and began stretching those instead. It took 9 months, a patent for the ’cold-drawing’ process of making fibres by removing them from the water of condensation, and 80 new polyamides before the most promising, nylon-6,6, was discovered in May 1934.

Nylon, a dyeable, durable, shiny thermoplastic first entered the market in 1938 as the bristles of a toothbrush, before being appropriated for women’s hosiery in 1940. DuPont declined to trademark the name ‘nylon’, instead allowing it to enter the lexicon as an alternative name for ‘stockings’. The new ‘nylons’ were a huge success. Nowadays, this fantastic fabric, which leaves a lower carbon footprint than wool, is used for meat wrappings, instrument strings and carpets, amongst many other things. Its only downside is its toxicity upon heating: it melts rather than burns, and breaks down to produce hydrogen cyanide.

This is ironic, actually, because Carothers never got to see his creation take hold. In 1937, just as his achievements were being celebrated and developed, he committed suicide with cyanide. He had suffered with depression and was grieving for the loss of his sister, but his suicide came as a shock. The suicide has been described as an ‘embarrassment’ for DuPont, and records relating to Carothers were lost or destroyed. This may help to explain why the discovery of nylon has since been wrapped in myth and mystery.

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Categories: Education

A short time ago in a journal not so far, far away…

Chemistry World blog (RSC) - 18 September, 2014 - 13:16

Guest post from Tom Branson

Inside Back Cover: Selective Targeting of Tumor and Stromal Cells By a Nanocarrier System Displaying Lipidated Cathepsin B Inhibitor (Angew. Chem. Int. Ed. 38/2014)
Angewandte Chemie International Edition
Volume 53, Issue 38, pages 10251-10251, 22 JUL 2014
DOI: 10.1002/anie.201406845
http://onlinelibrary.wiley.com/doi/10.1002/anie.201406845/full#car1

Science fiction often predicts future advances and has even prompted the development of some technologies. So should we be taking advantage of this association? Can we use a science fiction setting to showcase science fact? That idea is exactly what the latest cover of Angewandte Chemie has attempted to do.

It’s a trap!

There may be some of you who don’t immediately recognise the image above. It’s an homage to a scene in the Star Wars movies, where the plucky rebel alliance (piloting the small x-wing fighters) mount an attack on the Death Star, a moon-sized weapon of mass destruction and flagship of the evil empire. Hijacking this iconic scene is a certain way to grab the attention (George Lucas himself used it twice), especially by tapping into the current hype for the forthcoming films. But there doesn’t immediately appear to be a solid link between the rebel’s cause and Angewandte’s publishing ideals. In this case I’m not sure if the cover image really works to enhance and explain the research or actually provides a distraction from the science within. It’s certainly a fun image and a good way to get instant recognition of an idea, especially with fans of the franchise. That idea being the destruction of the evil empire, or in this case, evil cells.

In this interpretation the x-wing fighters have their own force fields and are carrying pills towards the Death Star, which itself looks to be in a dire state probably due to the growths in its innards. It should be a straightforward mission as long as the ships watch out for rogue fluorescing cells and a giant-lipidated-space-peptide.

This cover is very similar to an example from 2012 that also showed up in Angewandte. In both cases the empire, represented by the Death Star, took a beating, suggesting that there’s no sympathy for the Sith in the scientific community. For balance, I’d like to see someone’s interpretation of a Death Star nanoparticle destroying the peaceful bacterial population of Alderaan (I will accept joint authorship).

Stay on target

I love all things Star Wars (excluding Jar Jar Binks, of course) but this latest tie in to the franchise does seem a little out of place with the expanded Star Wars universe. No mention of carbonite or even ion cannons. But it does hint at the true content of the article: a new targeted drug delivery method. The group led by Boris Turk and Olga Vasiljeva from the Jožef Stefan Institute in Slovenia, have developed lipid vesicles conjugated to peptides that target extracellular cathepsin B (CtsB). CtsB is a cysteine protease that only translocates to the cell surface during cancer progression and is therefore a cancer-specific target. The research showed fluorophores and anticancer drugs could be transported in their vesicles and target the tumour environment.

For more about targeting cancer and less about the rebel alliance’s struggle, have a look at Angewandte Chemie.

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Categories: Education

WebElements: the periodic table on the WWW [http://www.webelements.com/]

Copyright 1993-2011 Mark Winter [The University of Sheffield and WebElements Ltd, UK]. All rights reserved.