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.
There 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.
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.
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.
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).
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!
1: J. D. Bernal: The Sage of Science. Andrew Brown, Oxford University Press, 2005
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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.
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.
Congratulations to all of our ISACS Chemistry World poster prize winners this year. Here’s a run-down of the winners:
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, 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, 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.
Guest post by Rowena Fletcher-Wood
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.
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