Justin’s research has garnered an international reputation for innovative biophysical chemistry approaches based on combining mass measurement with other experimental methods, simulations, and quantitative thermodynamic and kinetic analyses. This has allowed him and his group to change our thinking as to how proteins assemble, interact, and even evolve.
His group’s research impacts broadly the interface between chemistry and the life sciences. Their insights have been important to understanding molecular chaperone (mal)function in humans, and the stress tolerance of plants; and their innovations in mass measurement approaches have provided new means for researchers to quantify biomolecules and their interactions.

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Prof. Marcelo Guerin is the head of the Structural Glycobiology Lab at the Technological Park of Bizkaia, the Basque Country, Spain. He is particularly interested in investigating structural and mechanistic aspects of carbohydrate modifying enzymes. To this end, the group is using a multidisciplinary approach including X-ray crystallography, X-ray free electron laser and Cryo-electron microscopy.

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Malene R. Jensen is CNRS research director at the Institut de Biologie Structurale in Grenoble. She uses nuclear magnetic resonance (NMR) spectroscopy to study functional protein dynamics. She is mainly interested in understanding the role of large intrinsically disordered proteins in cell signalling.

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Cameron Mackereth is an Inserm research director, whose group is located at the Institut Européen de Chimie et Biologie at the University of Bordeaux. He uses NMR spectroscopy coupled with a variety of biophysical, in vitro and cell biology techniques to study the interaction between proteins and RNA. A major theme in the group is the molecular study of alternative splicing related to development and disease.

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Anna Moroni works at the Department of Biosciences of the U. of Milan, Italy. She investigates a class of membrane proteins, ion channels, with the aim of understanding the conformational changes leading to pore gating. To this end, she applies a combination of structural, functional and protein engineering approaches.

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Jean-Paul Renaud had been a CNRS research director at IGBMC in Illkirch, where he worked on nuclear receptors using X-ray crystallography. In 2002 he co-founded NovAliX, an innovative CRO offering an extensive structural biology and biophysics platform for
early-stage drug discovery. In 2015, he co-founded Urania Therapeutics(formerly RiboStruct) to leverage the know-how on eukaryotic ribosome crystallography built up by Marat Yusupov and Gulnara Yusupova at IGBMC to develop drug candidates targeting the human ribosome following a structure-based drug design approach.

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The Reuter group uses protein bioinformatics and molecular simulations to investigate protein dynamics. In particular we are interested in peripheral protein-lipid interactions at membrane interfaces and in conservation of protein flexibility within and across protein families. The Reuter group is at the University of Bergen (Norway) and affiliated to both the Chemistry Department and the Computational Biology Unit.

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Helen Saibil is a structural biologist at the Institute of Structural and Molecular Biology, Birkbeck College London. Her main interests are in analyzing conformational changes in macromolecular machines, mainly using cryo-electron microscopy and image processing. This work has focused on the actions of molecular chaperones in protein misfolding, aggregation and disaggregation in vitro and in cells, and on mechanisms of membrane pore formation in host-pathogen interactions.

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Pr. Claus Seidel heads the Chair for Molecular Physical Chemistry at the Heinrich-Heine-University Düsseldorf, Germany. He uses fluorescence spectroscopy with single-molecule detection and super-resolution microscopy combined with Förster Resonance Energy Transfer (FRET) measurements to study the dynamics and function of biomolecules and their assemblies in vitro and in live cells. In an integrative approach, the fluorescence studies are combined with other experimental biophysical techniques (NMR- and EPR-spectroscopy and SAXS) as well as with computer simulations to reach a more complete perspective on the dynamic personality and molecular function of proteins and nucleic acids. This dynamic view in a time range from picoseconds to minutes complements the traditional structure determination showing many detailed static snapshots of biomolecular structures.

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Charlotte Uetrecht studied biochemistry at the University of Potsdam, Germany. She performed her doctoral work in the group of Albert Heck at Utrecht University, the Netherlands. An EMBO longterm fellowship funded her postdoc in Uppsala, Sweden, and at European XFEL, Germany, where she is still working as guest scientist. Since 2014, Charlotte runs her own group at Heinrich Pette Institute, Leibnz Institute for Experimental Virology in Hamburg, Germany. She is well-known for structural, especially native, mass spectrometry of viruses and developing native mass spectrometry as delivery system for X-ray based structure determination.

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