June 2015



On the idyllic island of Lindau, Germany, you can’t help but be inspired by the beautiful vistas that envelope this small getaway on the edge of Lake Constance, with the town itself embodying the very spirit of the scientific meeting that is currently taking place here.

Nobel laureates (l-r) Eric Betzig, Stefan Hell, William Moerner, Martin Chalfie and Steven Chu discuss the nature of interdisciplinarity at the 65th Lindau Nobel meeting. Credit: Christian Flemming/Lindau Nobel Laureate Meetings

At the 65th Lindau Nobel Laureate meeting, 65 Nobel laureates from an array of scientific disciplines are hoping to inspire over 650 young scientists from across the world. These early career researchers have been selected from a vast amount of applicants to engage in scientific debate, foster new working relationships and gain inspiration from those who have dared to challenge scientific paradigms.

Delegates were treated to a series of fascinating talks on Monday morning from some of the most recent recipients of the famed Nobel medal. Stefan Hell and Eric Betzig, two recipients of the 2014 Nobel prize in chemistry for their work on super-resolution microscopy, kicked things off in earnest with frank discussions on how they arrived at this point. Hell’s talk in particular resulted in a poignant moment where he confessed that ‘it’s not the 2015 me who started this, but the 1990 me – he deserves the credit’. (more…)

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Guest post by Heather Cassell

Some experiments fail. Despite your best efforts, and especially for experiments that take many steps or a long time to run, you often won’t find out if they have worked until the very end.

Image By Tweenk (Own work) [CC BY 3.0], via Wikimedia Commons

As I’m sure you can imagine, this is a source of great frustration for a lab-based scientist. So much of your time is dedicated to setting up and running your experiment. Once you’ve made a plan and began the experiment, you have no choice but to blindly carry on assuming everything is fine, before you reach the end and discover whether or not it has worked. If it had then great! You can get on with the important business of analyzing your results to see how they fit in with the rest of your work. If your experiment didn’t work, you need to start the tortuous process of troubleshooting to find out what went wrong.

I have to confess that I enjoy the in between steps, the calm before the storm. There is a certain happiness in not knowing, freeing you up to concentrate on each step of your work, rather than the overall result. At this stage there is positivity and hope that your meticulous planning is going to give you the results you need. This positive attitude can last right up until the results come in, when the illusion can be shattered by the lovely picture of your positive controls and not much else.

So what to do now? Small changes to one of the steps in your process can make a huge difference to your results. Having a good set of both positive and negative controls can be a great help during troubleshooting: if the results show just your positive controls you know the problem is with your samples, if there are no results you know the problem is with the experiment. Now where will I find that error?

It is even more frustrating if you have inherited the protocol, or are trying to replicate one given in a paper. Even worse is a failing in a method you’ve had success with in the past! You can resolve many problems with patience and dedication, but sometimes it’s worth running the problem by someone else just to check you are not making a simple mistake that you have overlooked. Is the incubator at the wrong temperature? Have you added the wrong antibiotic? (Both common sleep deprivation related problems.)

You can spend days, weeks, even months tweaking the conditions of your experiment to make it work. But it is important that you don’t keep going round in circles or blindly repeating yourself, take notes, take a step back or take a deep breath and ask for help! Everyone has bad days in the lab, it’s how you react to them that shows how well suited you are to science.

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Guest post by Rowena Fletcher-Wood

Some discoveries are made after hunting hard for the answer, some come to you when you need them most, and some just turn up at parties. Such was the discovery of modern anaesthetics.

Method of administering nitrous oxide used by Samuel lee Rymer in London, 1863
Credit: Wellcome Library, London. Copyrighted work available under Creative Commons Attribution only licence CC BY 4.0

The concept of anaesthetics and their application to relieve pain during surgery was not wholly new. The Mesopotamians used alcohol (and its use persisted in resource deprived times such as war as late as 1812) and the ancient Chinese used acupuncture. The Sumerians may have used opium and Egyptians mandrake, and around a similar time, juniper and coca were put the the same use.

A popular anaesthetic in England between ~1200 and 1500 was Dwale – a mixture of varying composition containing opium and hemlock as well as lettuce, bile and bryony. Mandrake roots were chewed, extracting the active ingredients in doses that varied with chewing time or vigour. This was a risky business: low doses were often insufficient to fully mask the pain of surgery or put the patient to sleep, but at doses not much higher, many of these substances would become fatally toxic. Enough to make you numb just thinking about it. (more…)

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Guest post from Tom Branson

The taste of sweet success! But what is that flavour exactly, chewing gum or bon bons? The latest Organic & Biomolecular Chemistry (OBC) issue comes covered with sugary carbohydrate goodness and fullerene balls. Not at first obvious partners but throw in some lectins and you’ve got a hit.

On the cover a gumball machine has been set up in the lab with a few of the tasty C60 balls spilling out across the bench. The test tubes arranged at the back signify that the green, blue, red and yellow balls are obviously full of artificial colourings to make them tempting, but these are not for human consumption. In fact they are meant for bacterial consumption.

The bacteria in question produce fucose binding proteins, carbohydrate receptors that can be targeted for therapeutic reasons. On the cover, a schematic has been left out on the lab bench showing the fullerenes modified with linkers and terminating in fucose units, which then have a multivalent effect binding to one or more of the proteins.

The work focuses on the inhibition of two fucose binding proteins with very different binding site geometries. (more…)

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Guest post by JessTheChemist

’Many scientists, I think, secretly are what I call “boys with toys.”’

This poorly conceived comment by Shrinivas Kulkarni, an astronomy and planetary science professor at the California Institute of Technology, was made on National Public Radio (NPR)  and within hours, Twitter was abuzz with activity. Using the hashtag #girlswithtoys, female scientists from all over the world began posting pictures of themselves with their ‘toys’ – from telescopes to distillation kits to robots – to show that girls are scientists with fun toys too! This flippant comment highlights the unconscious bias that is all too common in the science world as it perpetuates the notion that science is a man’s world. The list of Nobel prize in chemistry winners also reflects this attitude, with only four females having won the prize to date. Of course, there have been many highly influential and talented women who were worthy of prize.

Blue plaque on SW10, Drayton Gardens, Donovan Court
By Gareth E Kegg – CC-BY-SA

This month’s blog will concentrate on the unsung hero of the discovery of the structure of DNA, Rosalind Franklin. Franklin’s x-ray diffraction images, which implied a helical structure for DNA, were key in determining the structure of DNA. James Watson and Francis Crick used this information in their Nature publication in 1953, where they gave Franklin and Maurice Wilkins an acknowledgement for their contributions. In 1962, Watson, Crick and Wilkins won the Nobel prize in physiology or medicine for their work on the structure of DNA but Franklin was left empty handed. Franklin died in 1958 and only living people can win the Nobel prize, so sharing the 1962 Nobel prize was not possible. However, the Nobel archives show that no one ever nominated her for the prize in physiology or medicine, or even the chemistry prize, despite the fact that her findings were undoubtedly significant to the discovery. (more…)

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