Marc Baldus | |
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Occupation | Professor of NMR spectroscopy |
Employer | Utrecht University |
Known for | Solid-state nuclear magnetic resonance, Structural biology |
Marc Baldus is a physicist and professor of NMR spectroscopy at Utrecht University. He is especially known for his work in the field of structural biology using solid-state nuclear magnetic resonance (ssNMR) spectroscopy. He applies ssNMR methods to establish structure-function relationships in complex biomolecular systems including membrane and Amyloid proteins. In addition, he develops cellular NMR methods to study large molecular transport and insertion systems in bacteria as well as signal transduction mechanisms in eukaryotic cells.
Marc Baldus studied physics at the Technische Universität Darmstadt, after which he became a Diploma Student at the Department of Physics of University of Florida in Gainesville, USA. He obtained his PhD degree in 1996 from the ETH Zurich in Switzerland. After postdoctoral research at MIT and Leiden University he became group leader at the Max Planck Institute for Biophysical Chemistry in Goettingen, Germany. In 2008 he became Full Professor of Structural Biology in the Bijvoet Centre for Biomolecular Research at Utrecht University in Utrecht. [1] From 2016 to 2019 he was scientific director of the Bijvoet Centre for Biomolecular Research. [2]
Marc Baldus is an expert in the field of structural biology using solid-state nuclear magnetic resonance (ssNMR) spectroscopy. In addition, he develops cellular NMR methods for structural biology, such as Dynamic Nuclear Polarization (DNP) NMR spectroscopy and his research group at Utrecht University was the first group worldwide with a 527 GHz Solid State DNP-NMR spectrometer. [3] [4] Baldus is also the coordinator of the uNMR-NL project, funded by the Netherlands Organisation for Scientific Research (NWO) with 18.5M Euro, to establish a national infrastructure for ultra-high field NMR spectroscopy, a joined initiative between Utrecht University, the Radboud University Nijmegen, Wageningen University, [5] Leiden University, [6] Eindhoven University of Technology and the Dutch public-private partnership COAST for the analytical sciences. [7] The uNMR-NL facility was officially opened by Dutch Undersecretary for Education, Culture and Science, Sander Dekker on November 5, 2015. [8] [9]
The main focus of the research of Marc Baldus is the use of solid state NMR spectroscopy [10] to study the structure and dynamics of proteins and other biomolecules. [1] He has used the technology amongst others to study the behavior of bacterial proteins, [11] [12] protein aggregation in Alzheimer's [13] and Parkinson's [14] disease, to study the effect of sugars on membrane behaviour, [15] for the analysis of membrane embedded proteins such as G-protein coupled receptors [16] [17] and ion channels [18] and for the characterization of novel drug delivery systems. [19] In recent years, his attention has been focussed on the analysis of in-cell NMR [20] to study the structure and function of proteins in their native cellular environment. [21]
Marc Baldus received the Founders Medal of the International Conference on Magnetic Resonance in Biological Systems (ICMRBS) in August 2006. [22] [23] [24] In 2014, Marc Baldus received the Günther Laukien Prize from Richard Ernst, 1991 Nobel laureate in Chemistry. The prize recognizes cutting-edge experimental NMR research, is awarded yearly and is one of the most prestigious prizes in the field of NMR and MRI. [25] [26]
Biophysics is an interdisciplinary science that applies approaches and methods traditionally used in physics to study biological phenomena. Biophysics covers all scales of biological organization, from molecular to organismic and populations. Biophysical research shares significant overlap with biochemistry, molecular biology, physical chemistry, physiology, nanotechnology, bioengineering, computational biology, biomechanics, developmental biology and systems biology.
Kurt Wüthrich is a Swiss chemist/biophysicist and Nobel Chemistry laureate, known for developing nuclear magnetic resonance (NMR) methods for studying biological macromolecules.
Nicolaas Bloembergen was a Dutch-American physicist and Nobel laureate, recognized for his work in developing driving principles behind nonlinear optics for laser spectroscopy. During his career, he was a professor at Harvard University and later at the University of Arizona and at Leiden University in 1973.
Hartmut Michel is a German biochemist, who received the 1988 Nobel Prize in Chemistry for determination of the first crystal structure of an integral membrane protein, a membrane-bound complex of proteins and co-factors that is essential to photosynthesis.
Solid-state NMR (ssNMR) spectroscopy is a technique for characterizing atomic level structure in solid materials e.g. powders, single crystals and amorphous samples and tissues using nuclear magnetic resonance (NMR) spectroscopy. The anisotropic part of many spin interactions are present in solid-state NMR, unlike in solution-state NMR where rapid tumbling motion averages out many of the spin interactions. As a result, solid-state NMR spectra are characterised by larger linewidths than in solution state NMR, which can be utilized to give quantitative information on the molecular structure, conformation and dynamics of the material. Solid-state NMR is often combined with magic angle spinning to remove anisotropic interactions and improve the resolution as well as the sensitivity of the technique.
Nuclear magnetic resonance spectroscopy of proteins is a field of structural biology in which NMR spectroscopy is used to obtain information about the structure and dynamics of proteins, and also nucleic acids, and their complexes. The field was pioneered by Richard R. Ernst and Kurt Wüthrich at the ETH, and by Ad Bax, Marius Clore, Angela Gronenborn at the NIH, and Gerhard Wagner at Harvard University, among others. Structure determination by NMR spectroscopy usually consists of several phases, each using a separate set of highly specialized techniques. The sample is prepared, measurements are made, interpretive approaches are applied, and a structure is calculated and validated.
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Adriaan "Ad" Bax is a Dutch-American molecular biophysicist. He was born in the Netherlands and is the Chief of the Section on Biophysical NMR Spectroscopy at the National Institutes of Health. He is known for his work on the methodology of biomolecular NMR spectroscopy.
Johannes Martin Bijvoet was a Dutch chemist and crystallographer at the van 't Hoff Laboratory at Utrecht University. He is famous for devising a method of establishing the absolute configuration of molecules. In 1946 he became member of the Royal Netherlands Academy of Arts and Sciences.
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Robert Guy Griffin is a Professor of Chemistry and director of the Francis Bitter Magnet Laboratory at Massachusetts Institute of Technology (MIT). He is known for his work in nuclear magnetic resonance and developing high-field dynamic nuclear polarisation (DNP) for the study of biological solids. He was awarded the ISMAR Prize in 2010 and the Günther Laukien Prize for NMR research in 2007. In 2018, he received the Bijvoet Medal of the Bijvoet Center for Biomolecular Research of Utrecht University
The Bijvoet Centre for Biomolecular Research is a research institute at Utrecht University. The Bijvoet Centre performs research on the relation between the structure and function of biomolecules, including proteins and lipids, which play a role in biological processes such as regulation, interaction and recognition. The Bijvoet Centre houses advanced infrastructures for the analysis of proteins and other biomolecules using NMR, X-ray crystallography, electron microscopy and mass spectrometry. The institute is named after famous Dutch chemist Johannes Martin Bijvoet, who worked at Utrecht University.
Joachim Heinrich Seelig is a German physical chemist and specialist in NMR Spectroscopy. He is one of the founding fathers of the Biozentrum of the University of Basel.
G. Marius Clore MAE, FRSC, FRS is a British-born, Anglo-American molecular biophysicist and structural biologist. He was born in London, U.K. and is a dual US/U.K. Citizen. He is a Member of the National Academy of Sciences, a Fellow of the Royal Society, a NIH Distinguished Investigator, and the Chief of the Molecular and Structural Biophysics Section in the Laboratory of Chemical Physics of the National Institute of Diabetes and Digestive and Kidney Diseases at the U.S. National Institutes of Health. He is known for his foundational work in three-dimensional protein and nucleic acid structure determination by biomolecular NMR spectroscopy, for advancing experimental approaches to the study of large macromolecules and their complexes by NMR, and for developing NMR-based methods to study rare conformational states in protein-nucleic acid and protein-protein recognition. Clore's discovery of previously undetectable, functionally significant, rare transient states of macromolecules has yielded fundamental new insights into the mechanisms of important biological processes, and in particular the significance of weak interactions and the mechanisms whereby the opposing constraints of speed and specificity are optimized. Further, Clore's work opens up a new era of pharmacology and drug design as it is now possible to target structures and conformations that have been heretofore unseen.
David Lyndon Emsley FRSC is a British chemist specialising in solid-state nuclear magnetic resonance and a Professor at EPFL. He was awarded the 2012 Grand Prix Charles-Leopold Mayer of the French Académie des Sciences and the 2015 Bourke Award of the Royal Society of Chemistry.
Hartmut Oschkinat is a German structural biologist and professor for chemistry at the Free University of Berlin. His research focuses on the study of biological systems with solid-state nuclear magnetic resonance.
Gerhard Wagner is a German-American physicist currently the Elkan Rogers Blout Professor of Biological Chemistry and Molecular Pharmacology at Harvard Medical School and is an Elected Fellow of the American Association for the Advancement of Science, German National Academy of Sciences Leopoldina, American Academy of Arts and Sciences, National Academy of Sciences and International Society of Magnetic Resonance. He is considered one of the pioneers in Biological Nuclear Magnetic Resonance (NMR) spectroscopy (Bio-NMR) and his research has been focused on protein structure, dynamics and stability, and on the relation of these to protein function. He is a structural biologist and is recognized for his work on the development of NMR spectroscopy for determination of protein structures in solution and characterizing protein dynamics.
Johannes Frederik Gerardus (Hans) Vliegenthart is a Dutch emeritus professor in bioorganic chemistry of Utrecht University, well known for his research on the synthesis and characterisation of carbohydrates, and biomolecules containing sugar moieties such as glycoproteins and their role in living cells.
Mei Hong is a Chinese-American biophysical chemist and Professor of Chemistry at the Massachusetts Institute of Technology. She is known for her creative development and application of solid-state nuclear magnetic resonance (ssNMR) spectroscopy to elucidate the structures and mechanisms of membrane proteins, plant cell walls, and amyloid proteins. She has received a number of recognitions for her work, including the American Chemical Society Nakanishi Prize in 2021, Günther Laukien Prize in 2014, the Protein Society Young Investigator award in 2012, and the American Chemical Society’s Pure Chemistry award in 2003.
The Cluster of Excellence Frankfurt “Macromolecular Complexes” (CEF) was established in 2006 by Goethe University Frankfurt together with the Max Planck Institute of Biophysics and the Max Planck Institute for Brain Research in the context of the German Universities Excellence Initiative. Funding by the Deutsche Forschungsgemeinschaft (DFG) endet in October 2019. CEF grew out of the long-standing collaborative research on membrane proteins and RNA molecules and strengthened research efforts in these fields by recruiting further scientists to Frankfurt/Main. CEF brought together the research activities of up to 45 research groups, the majority of which were based on Riedberg Campus in Frankfurt/Main. CEF founded the Buchmann Institute for Molecular Life Sciences (BMLS).