My name is Mark van Goor, a PhD candidate in the Physiology lab, which is part of the Renal disorders theme. I was born in Groningen, in 1991, to Marianne and Harry, and I have two little sisters (well, they’re 25 and 26 now) called Harriët and Ellen.
When you were a kid, what did you want to be when you grew up? Can you tell us something about your child years?When I was young, I wanted to become a dolphin trainer, professional football player, cook and architect all at the same time. However, after realizing that the odds of me becoming a dolphin trainer were close to non-existent, that I was only marginally talented in football and cooking, and that I needed to understand math to become an architect, I decided to push the decision to a much later date and to just focus on having fun at the Stedelijk Gymnasium in Nijmegen.
What was your previous academic training, where did you study and why that study?
I kind of stumbled into Biomedical Sciences at the Radboud University, after some short-lived spells at Molecular Life Sciences and Biology. I was contemplating becoming a physician, and at the time Biomedical Sciences was an almost surefire way to enroll in medicine. I soon realized that I enjoyed the puzzle of human biology way more than I enjoyed patient-focused healthcare, which is why I decided to stay in Biomedical Sciences. Although this choice sadly led me to forego any chance of a doctor’s salary, I am very passionate about fundamental research and it brings me a lot of joy.
The RIMLS motto is: ‘Today’s molecules for tomorrow’s medicine’. What does this mean for you?
My particular area of interest is in structural biology, which is a field that aims to elucidate the atomic structures of biological molecules, mainly proteins, to understand how they work as molecular machines. The RIMLS motto is very relevant in my field and mirrors current developments in structural biology. We’re now at a point where (membrane) proteins can be structurally resolved to a very high resolution, almost to the point where we can start to design new drugs through intelligent drug design. We’re close to literally designing new molecules for tomorrow’s medicine.
Who is your great example as scientists? And why?
I’ve always been fascinated by scientists that positioned themselves at the crossroads between multiple fields, borrowing and using concepts from math, physics, computer sciences and chemistry to solve the puzzles of biology. One such scientist was Richard Feynman, a nobel prize winner in Physics that was sympathetic to the slow progress that biologists were making in answering the fundamental questions of life, back in 1960. In a talk, titled: ‘there’s plenty of room at the bottom’, Feynman describes concepts that are nowadays commonplace, such as light-based communication between continents (internet), microchips and nanotechnology. But he also famously commented on the power of the electron microscope: “It is very easy to answer many of these fundamental biological questions; you just look at the thing!”. Stating that a 100x increase in the power of the electron microscope would allow unpresedented insights into biology. It turns out he was right, and we are now able to look at cells on the molecular level, answering some of our questions and revealing new challenges. Within my field of study, I admire the pioneers that have pushed cryo-electron microscopy to what it is today. Three of them were selected for the Nobel prize in Chemistry in 2017; Richard Henderson, Jacques Dubochet and Joachim Frank, who solved some of the fundamental challenges in sample preparation, microscope use and image analysis. I also deeply respect Yifan Cheng for the way he approaches science and the almost child-like enthusiasm he displays when discussing potential new avenues that we can take. All of these scientists have in common that they like to challenge existing concepts, approach science with a sense of wonder and awe, and that they dream big.
Which research discovery that you have made has made you most proud?I’ve really enjoyed solving the puzzle of how the renal calcium channel TRPV5 is inhibited by calcium and calmodulin and that we were able to show an inhibited state of the channel in molecular detail. The paper that came out of this project is the culmination of three years of work and is my first foray in the field of structural biology. I hope to be involved in many more exciting discoveries in the future!
Given unlimited finance what experiment would you perform?I would solve the structure of everything. To me, the cell is just an extremely extensive machine that we can learn to understand. Right now, we’re using structural biology to understand single cogs within the machinery, but we are unsure as to how these cogs fit together to perform a function. In the future, the focus will be on deciphering how these cogs fit together to produce biologically relevant outcomes, which involves solving the structures of protein complexes and modelling dynamics. In the end, we should be able to describe an entire cell in terms of its machinery. Indeed, efforts are being made to structurally characterize entire cells, using focused ion beam milling to reveal the interior of the cell and machine learning to map the contents. The resolution of this technique is still limited and is also performed on fixed cells which makes it impossible to study dynamics.
What does your working area look like and what does it say about you or your research?My desk is actually quite tidy. I like to keep it that way because I’m usually all over the place. Having a tidy desk allows me to be a little bit chaotic in my way of thinking while ensuring that I still perform experiments in a neat manner. If my desk was a complete mess, I would start to make a lot more mistakes.
Nominate a colleague to be in the spotlight:I would like to nominate René Bindels, and I would like to ask him what he thinks retirement will be like and what he will focus his passion on. My dad is about the same age and he’s thinking a lot about this question at the moment.
What type of person are you? Quick insights:a) Mac or PC? : How is this even a question? 1000 euro for a pretty apple screen stand with no added functionality, ehm no thanks?
b) Theater or cinema? : Cinema
c) Dine out or dine in? : Dine out, although I do enjoy cooking
d) Ferrari or Fiat? : Ferrari
e) Shopaholic or chocoholic? : Neither really
f) Culture or Nature : Nature
Related news items
RIMLS award ceremony proudly presenting the winners16 January 2020
Several RIMLS researchers received an award and bonus during the New Year's drinks. See all photo's and the ENABLE aftermovie.read more
Stofwisselkracht grant for Daan Panneman and Richard Rodenburg16 January 2020
Daan Panneman & Richard Rodenburg have been awarded a Stofwisselkracht grant for their proposal “CRISPR/Cas9 knock-in complementation in fibroblasts of mitochondrial disease patients”. Together with Omar Tutakhel & Jan Smeitink they will investigate the possibility of using CRISPR/Cas9 knock-in.read more
Radboud Talks 2020 scientific pitch competition14 January 2020
The next edition of Radboud Talks will take place in the spring. During this academic pitch competition, young researchers will be given the opportunity to share their stories with a large audience. In a three-minute presentation, you will talk about your research in a fun and accessible manner.read more
Rubicon Grant for Sami Mohammed14 January 2020
Former RIMLS researcher Sami Mohammed, theme Renal disorders, received a Rubicon Grant from the Dutch Organisation for Scientific Research (NWO). The Rubicon program gives young, highly promising researchers the opportunity to gain international research experience.read more
Review Sanne Frambach accepted by Pharmacological Reviews13 January 2020
In this review entitled 'Brothers in arms: ABCA1 and ABCG1-mediated cholesterol efflux as promising targets in cardiovascular disease treatment', RIMLS researcher Sanne Frambach, describe the possibilities for stimulating cellular efflux.read more
p120-catenin-dependent collective brain infiltration by glioma cell networks7 January 2020
Pavlo Gritsenko and Peter Friedl, theme Cancer development and immune defense, report in Nature Cell Biology, that glioma cells infiltrate the brain by a collective network mechanism, which critically depends on p120 catenin. p120 thus represents a potential target to combat glioma.read more