Jérôme Boisbouvier

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Advanced isotopic labeling for the NMR investigation of challenging proteins and nucleic acids

Jerome Boisbouvier, Lewis E. Kay

Journal of Biomolecular NMR > 2018 > 71 > 3 > 115-117

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Observation of CH⋅⋅⋅π Interactions between Methyl and Carbonyl Groups in Proteins

Frédéric A. Perras, Dominique Marion, Jérôme Boisbouvier, David L. Bryce, more

Angewandte Chemie International Edition > 56 > 26 > 7564 - 7567

Protein structure and function is dependent on myriad noncovalent interactions. Direct detection and characterization of these weak interactions in large biomolecules, such as proteins, is experimentally challenging. Herein, we report the first observation and measurement of long‐range “through‐space” scalar couplings between methyl and backbone carbonyl groups in proteins. These J couplings are indicative...

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Observation of CH⋅⋅⋅π Interactions between Methyl and Carbonyl Groups in Proteins

Frédéric A. Perras, Dominique Marion, Jérôme Boisbouvier, David L. Bryce, more

Angewandte Chemie > 129 > 26 > 7672 - 7675

Protein structure and function is dependent on myriad noncovalent interactions. Direct detection and characterization of these weak interactions in large biomolecules, such as proteins, is experimentally challenging. Herein, we report the first observation and measurement of long‐range “through‐space” scalar couplings between methyl and backbone carbonyl groups in proteins. These J couplings are indicative...

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Methyl-specific isotopic labeling: a molecular tool box for solution NMR studies of large proteins

Rime Kerfah, Michael J Plevin, Remy Sounier, Pierre Gans, more

Current Opinion in Structural Biology > 2015 > 32 > Complete > 113-122

Nuclear magnetic resonance (NMR) spectroscopy is a uniquely powerful tool for studying the structure, dynamics and interactions of biomolecules at atomic resolution. In the past 15 years, the development of new isotopic labeling strategies has opened the possibility of exploiting NMR spectroscopy in the study of supra-molecular complexes with molecular weights of up to 1MDa. At the core of these isotopic...

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CH₃-specific NMR assignment of alanine, isoleucine, leucine and valine methyl groups in high molecular weight proteins using a single sample

Rime Kerfah, Olivier Hamelin, Jérôme Boisbouvier, Dominique Marion

Journal of Biomolecular NMR > 2015 > 63 > 4 > 389-402

A new strategy for the NMR assignment of aliphatic side-chains in large perdeuterated proteins is proposed. It involves an alternative isotopic labeling protocol, the use of an out-and-back ¹³C–¹³C TOCSY experiment ((H)C-TOCSY-C-TOCSY-(C)H) and an optimized non-uniform sampling protocol. It has long been known that the non-linearity of an aliphatic spin-system (for example Ile, Val, or Leu) substantially...

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Scrambling free combinatorial labeling of alanine-β, isoleucine-δ1, leucine-proS and valine-proS methyl groups for the detection of long range NOEs

Rime Kerfah, Michael J. Plevin, Ombeline Pessey, Olivier Hamelin, more

Journal of Biomolecular NMR > 2015 > 61 > 1 > 73-82

Specific isotopic labeling of methyl groups in proteins has greatly extended the applicability of solution NMR spectroscopy. Simultaneous labeling of the methyl groups of several different amino acid types can offer a larger number of useful probes that can be used for structural characterisations of challenging proteins. Herein, we propose an improved AILV methyl-labeling protocol in which L and...

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Bestimmung transienter Konformationszustände von Proteinen durch Festkörper‐R_1ρ‐Relaxationsdispersions‐NMR‐Spektroskopie

Peixiang Ma, Jens D. Haller, Jérémy Zajakala, Pavel Macek, more

Angewandte Chemie > 126 > 17 > 4400 - 4405

Die Funktion von Proteinen basiert auf der Fähigkeit, eine Vielfalt an Zuständen einzunehmen, die sich in ihren Strukturen und freien Energien unterscheiden. Um eine Proteinfunktion zu verstehen, gilt es daher herauszufinden, wie die verschiedenen, thermisch zugänglichen Konformationen miteinander verbunden sind und welche Strukturen und relativen Energien sie aufweisen. Viele biomolekulare Reaktionen...

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Frontispiz: Bestimmung transienter Konformationszustände von Proteinen durch Festkörper‐R_1ρ‐Relaxationsdispersions‐NMR‐Spektroskopie

Peixiang Ma, Jens D. Haller, Jérémy Zajakala, Pavel Macek, more

Angewandte Chemie > 126 > 17 > n/a - n/a

In der Zuschrift auf S. 4400 ff. beschreiben P. Schanda et al. eine NMR‐Methode, die den Nachweis kurzlebiger Proteinzustände ermöglicht. Informationen über die Austauschkinetik, relativen Besetzungen und Strukturen der Zustände können gewonnen werden.

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Probing Transient Conformational States of Proteins by Solid‐State R_1ρ Relaxation‐Dispersion NMR Spectroscopy

Peixiang Ma, Jens D. Haller, Jérémy Zajakala, Pavel Macek, more

Angewandte Chemie International Edition > 53 > 17 > 4312 - 4317

The function of proteins depends on their ability to sample a variety of states differing in structure and free energy. Deciphering how the various thermally accessible conformations are connected, and understanding their structures and relative energies is crucial in rationalizing protein function. Many biomolecular reactions take place within microseconds to milliseconds, and this timescale is therefore...

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Frontispiece: Probing Transient Conformational States of Proteins by Solid‐State R_1ρ Relaxation‐Dispersion NMR Spectroscopy

Peixiang Ma, Jens D. Haller, Jérémy Zajakala, Pavel Macek, more

Angewandte Chemie International Edition > 53 > 17 > n/a - n/a

In their Communication on page 4312 ff., P. Schanda et al. describe an NMR method used to probe conformational states of proteins. Information about the exchange kinetics, relative populations, and structures of the short‐lived state can be obtained.

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Specific labeling and assignment strategies of valine methyl groups for NMR studies of high molecular weight proteins

Guillaume Mas, Elodie Crublet, Olivier Hamelin, Pierre Gans, more

Journal of Biomolecular NMR > 2013 > 57 > 3 > 251-262

The specific protonation of valine and leucine methyl groups in proteins is typically achieved by overexpressing proteins in M9/D₂O medium supplemented with either labeled α-ketoisovalerate for the labeling of the four prochiral methyl groups or with 2-acetolactate for the stereospecific labeling of the valine and leucine side chains. However, when these labeling schemes are applied to large protein...

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