Scientific research is hard …so you have to enjoy it!

Today we’re talking to Tim Donohoe, Professor of Chemistry at the University of Oxford and Editor of Tetrahedron Letters.

What are your research interests/describe a typical working day
“I research organic chemistry in the broadest sense, but am particularly interested in total synthesis and catalysis.” Tim leads a research team of 16-20 people, a mixture of graduates/undergraduates plus postdoctoral researchers. “My job is to support them and together do the best research possible.” As well as this, Tim is also responsible for teaching and has various administrative duties. What’s more, he’s also an editor for Tetrahedron Letters! 

How do you measure success in your work?
“One thing that gets my fist pumping is when we get a really nice piece of work accepted for publication. Or when a grant gets funded – we can then do more research! Another thrill is when a member of the group gets a job (especially if it’s in chemistry!).”

Do you have any particular advice for younger researchers?
“Scientific research is hard”, says Tim “…so you have to enjoy it! The opportunity to have a job you enjoy is a privilege. If you enjoy it, work at it to be best you can be. Read widely. Make sure you are good at communicating science – presentations, writing at the board and that sort of thing.”

What drove you to become an Editor?
“I was invited!” Tim started his editorial work with the journal in January 2014. 

What is the most rewarding aspect of editorial work for you and what do you find difficult about the role?
In terms of reward, Tim finds it pleasing to be able to “help get great science published”. He sees his job to help the journal and grow its reputation. He also likes helping researchers around the world. “It’s great to see a manuscript coming back with helpful referees’ comments, then see the improvements in the revised version.” What’s not so good is having to make difficult decisions. Sometimes papers are “in the middle” – which way to go? Occasionally referees’ comments are short and unhelpful to both the author and the editor – so then one’s left in a quandary. 

What professional use (if any) do you make of social media and/or scholarly collaboration tools like Mendeley?
Tim does make use of some tools. Not much social media though. Tim finds Mendeley helpful to share ideas with other editors and Elsevier staff: the group discussion aspect is useful. “At the TET conference in Budapest – we had a virtual poster symposium. You could join the [Mendeley] group and look at the science that was being presented. You could comment and interact, even from home. That was great as it gave those unable to attend a chance to participate.” Tim doesn’t use Twitter as an active user but browses journals’ feeds.

If we could build a tool/device to help you most in your career or editorial work; what would it be?
If we’re looking at a scientific demand then something that would help organic chemistry research, in particular catalytic reactions. “There’s a lot going on in a catalytic reaction. If a particular reaction doesn’t work, we don’t know why. What we need is a simple way of working out WHY: some way of interrogating unsuccessful interactions!”

Have you any particular interests in what remains of your time apart from university and editorial work?
“Family! Squash. And I go to the gym to keep fit.”

Tim was interviewed by Christopher Tancock

2017 Reaxys PhD Prize

Open for Submissions: the 2017 Reaxys PhD Prize

Today marks an important day in the chemistry calendar: the launch of the 2017 Reaxys PhD Prize! From now until March 13, talented and ambitious chemistry PhD students from all around the world will be sending their submissions, all hoping to show the Review Board that they deserve a place on the list of finalists.

It’s considered a high honor to be a Reaxys PhD Prize finalist. Each entry is judged in terms of originality, innovation, importance and applicability of the research. The reviewers also look at the rigor of approach and methodology and the quality and clarity of related publications. Recommendation letters and CVs are also considered. Hundreds of applications come in each year, with students from over 400 institutions having participated to date, and the Review Board have consistently praised the quality of the submissions.

It is the Review Board’s task to select the 45 finalists, who are invited to present their research at the Reaxys PhD Prize Symposium. This year’s event will be held in Shanghai in October, with travel bursaries and accommodations provided to ensure that the finalists can attend. The 2016 symposium was in London—you can see the highlights in this short video:

In addition to gaining recognition for their research excellence and an opportunity to present their work, all the finalists are invited to join the Reaxys Prize Club, a unique, international network of chemists from all researchers and career paths. Now with over 300 members, the Club has proven to boost the careers of young chemists, helping them to meet with other chemists, attend conferences, and organize events. Prize Club members also receive personal access to Reaxys and Reaxys Medicinal Chemistry and discounts on Elsevier books.

Being a finalist is an accolade in itself, but the participants all certainly hope to be selected as one of the three winners. The shortlisted best finalists make a final oral presentation of their research at the Reaxys PhD Prize Symposium, based on which, the Review Board Chairs select the winners. Each winner receives a prize of $2000 in addition to all the benefits that finalists get.

The competition is open to anyone who has just finished or is currently engaged in a PhD program where the research focus is related to chemistry. Previous finalists have hailed from institutions in Asia, the Americas, Europe and the Middle East—and they are all members of the Reaxys Prize Club, meaning it is a global network of dedicated and talented chemists.

Could you or someone you know be one of this year’s finalists? All the details about applying can be found here.

JoVE Guest Blog Post – Visualising Scientific Experiments

JoVE October blog

This is the first in a series of guest posts from JoVE, the Journal of Visualized Experiments. Each month we’ll be featuring a different peer-reviewed video article with insights from their team. Like Mendeley, JoVE is using technology to make science more open, and we were really happy to have their Director of Marketing Rachel Greene join us at Social Media Week London for the Mendeley Masterclass on How Technology is Changing Research. You can watch the video of her presentation, talking about how visualising experiments enhance reproducibility on the Mendeley YouTube channel, and as usual let us know what you think in the comments below!

MALDI-TOF MS, an Adaptable Method for Protein Characterization, Visualized in a JoVE-Chemistry Video Article

(J. Vis. Exp. (79) e50635, doi:10.3791/50635 (2013))

By Val Buntrock, Ph.D.

Journal Development Editor, JoVE

A recent video-article published in JoVE, the Journal of Visualized Experiments, by a research group at the Centre National de la Racherche Scientifique (CNRS) captures the process of analyzing intact proteins using mass spectrometry (MS). In their video article, Signor et al. demonstrate how to accurately measure large proteins using matrix assisted laser-desorption ionization time-of-flight (MALDI-TOF) MS. Often, when describing MALDI-TOF MS procedures in text, essential information is omitted, leading to poor reproducibility. Part of a new trend in publishing, this video demonstration records the subtleties and nuances of this complex technique. Employing proper technique and variable consideration, this research group identifies an intact, large protein (> 100 kDa) with high sensitivity using a small amount (0.5 pmoles) of protein sample. Using these video instructions, research groups around the globe can modify this flexible technique to identify an infinite number of large proteins.

Phosphoregulation

Characterizing proteins is important for determining the current state of the protein, which has severe implications to several biological processes. The significance of proteins switching between active and inactive forms via protein kinase phosphorylation events has been recognized and applied to cellular and molecular research for several decades. Researchers have gone on to show that protein folding, as determined by phosphorylation, either exposes or protects structural motifs that serve as binding sites for effector molecules. Further, the binding between protein and effector molecule controls protein function. Therefore, the initial protein phosphorylation event regulates the activity level of the protein.

Protein activity or function plays a role in switching on or off a large number of cellular processes, such as cell communication and cell replication. As structural biologists identify a growing number of disease states related to malfunctioning protein modifications and subsequent de-regulation, understanding and identifying the differences between the two states of the protein (active or inactive) has become a priority.

Protein Characterization

A simple, fast, and common method of determining the presence or absence of phosphorylation in proteins is by determining their mass using mass spectrometry (MS). MS ionizes the molecule of interest, generating a charged species, and measures its mass-to-charge or m/z ratio.  The m/z ratio is determined by the isotopic distribution of each element present, meaning that each molecule or protein has its own unique isotopic pattern or fingerprint.

Two MS techniques are typically used to ionize heavy and labile biomolecules, such as proteins: electrospray ionization (ESI MS) and matrix assisted laser-desorption ionization time-of-flight (MALDI-TOF MS). ESI MS analysis requires dissolution of the sample in a pure solvent for direct ionization from the solution mixture. MALDI-TOF MS utilizes a co-crystallization method wherein the protein is crystallized with an ultraviolet (UV) absorbing organic species. This organic molecule is referred to as the matrix molecule or substance.

While ESI MS is more sensitive and accurate, the instrument compatible solvents or buffers typically contain significant amounts of substances, such detergents and salts, which interfere with the desired protein pattern. Additionally, ESI MS data is more difficult to interpret given that ESI MS spectra are riddled with multiple overlapping charge states from a single protein. A more gentle technique, MALDI-TOF MS produces fewer multiply-charged species, leading to a much cleaner spectra that is easier to analyze. This is especially true for larger biomolecules, such as proteins, which can fragment into numerous multiply charged species using ESI MS. For these reasons, MALDI-TOF MS is the preferred technique for protein analysis.

Optimizing MALDI-TOF MS Technique

Matrix

Purity at every stage of MALDI-TOF MS analysis is crucial to obtaining the highest quality MS spectra or protein fingerprint. For this reason, Signor et al. provide detailed instructions for how to effectively 1) clean the MALDI plate that holds the matrix and protein of interest and 2) purify the matrix substances using standard recrystallization techniques. Further, they employ two different matrix systems to compare which one yields the best results for the protein of interest. A single matrix and a mixed matrix system are used, demonstrating the influence of the matrix on the resulting spectra. In their work, Signor et al. found that the mixed matrix system yielded a higher signal to noise and a greater sensitivity than the single matrix system.

Deposition Method

The deposition method is another technique variable that impacts the quality of MALDI-TOF MS results. The two most commonly employed deposition methods are the droplet and thin layer method. Using a droplet technique, a mixture of the protein analyte and matrix solution is “dropped” onto the target substrate, and the solvent is evaporated, yielding a crystalline mixture of the matrix and protein. Slightly more controlled, the thin layer technique is composed of layers of matrix sandwiching the protein analyte layer. While the droplet method suffers from poor resolution and an inability to observe larger proteins (> 100 kDa), the thin layer deposition yields a protein fingerprint for large proteins, sharper peaks, and a higher signal to noise.

As protein analysis becomes a more vital component of studying protein modifications, mastering protein characterization techniques is increasingly important. In this video-article, Signor et al. provide a detailed overview of the steps involved in utilizing MALDI-TOF MS to analyze proteins. They also provide essential considerations and modifications to guide beginners and experts alike through tailoring this powerful technique to study different target proteins. Shown in video format, the necessary level of details, such as how to properly perform multiple deposition methods, is captured and relayed to the viewer for increased transparency.

 

 

 

 

Mendeley Investor Sponsors Annual Science Academy Prizes

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Image: http://www.nyas.org

Leonard Blavatnik – the Ukrainian-born billionaire from Access Industries who was one of the biggest investors in Mendeley before the acquisition by Elsevier in April – is continuing the trend of investing in research by backing the New York Academy of Sciences’ annual prizes for young scientists.

Tamar Lewin reported in a recent New York Times article that the scheme is building on the success of a smaller program that was piloted in New York, New Jersey and Connecticut over the past seven years. It will now award three prizes of $250,000 each in the areas of Physical Sciences & Engineering, Chemistry and Life Sciences.

It might not seem such a large amount when compared with the Nobel prize (which is currently around $1 million) or the whopping $3 Million that each winner of the newly established Breakthrough Prizes received, yet these awards are targeted towards younger up-and-coming researchers (there is an age limit of 42) rather than those that are already leaders in their field.

The idea, according to Blavatnik is to make the prizes big enough to be interesting but not so large as to be scary. While there are many rewards and incentives for established and prominent scientists, there are fewer initiatives to encourage and support young researchers in a sustained and more systematic way. The aim is to use this incentive to help spur the next generation of scientific innovators. Mr Blavatnik is a philanthropist with a keen interest in scientific research, having funded  the Blavatnik School of Government at the University of Oxford to the tune of $114 million and also recently donating $50 million to Harvard and $10 million to Yale.

Past finalists and winners of the regional Blavatnik Awards talk about how they were pivotal for their careers: Elisa Oricchio, a Research Fellow of the Cancer Biology & Genetics Program at the Memorial Sloan-Kettering Cancer Center says that the prize is a wonderful stimulus and confidence booster for young scientists and “identifies emerging scientific thought leaders and highlights their work to the broader scientific community.”

Nominations for the prize will come from around 300 leading medical centres and research universities and an advisory council of past winners, Nobel laureates and prominent scientists. The judging panel – made up of 60 distinguished scientists – will then select winners based on the impact, quality and novelty of their research. The first nominations will be accepted from September through December 2013, with winners being announced in September 2014.

“The long-term goal of the awards is to create a pipeline of scientific support in which established scientists choose the most outstanding young faculty-rank scientists, who then go on to mentor the next generation of would-be scientists and award winners,” said the president of the New York Academy of Sciences Ellis Rubinstein.

Do you think these prizes make a real difference towards advancing science and supporting researchers and their work? Mendeley and Elsevier are also looking at some interesting initiatives and awards to support early career researchers, so watch this space, and in the meantime let us know what you think!