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Chapitre D'ouvrage Année : 2012

Protein Dynamics in the Solid State

Résumé

An understanding of biological processes at the molecular level comes from knowledge of the atomic structures of biological macromolecules and how they change over time. Knowledge of molecular motions is consequently an indispensible ingredient for a detailed comprehension of the machinery of life. For example, dynamics is at the core of molecular recognition, signaling, ligand binding, catalysis, and folding phenomena. Moreover, dynamics controls the mechanical properties of structural biopolymers. NMR is a natural choice for studying dynamics, with a variety of possible observables that are sensitive to dynamics over timescales from 10−12 to 102 s. This chapter provides an elementary survey of how solid-state NMR can be used to study the dynamics of proteins.
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Dates et versions

hal-00809254 , version 1 (08-04-2013)

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Jozef R. Lewandowski, Lyndon Emsley. Protein Dynamics in the Solid State. I. Bertini, K. S. McGreevy and G. Parigi. NMR of Biomolecules: Towards Mechanistic Systems Biology, Wiley-VCH Verlag GmbH & Co. KGaA, pp.366-375, 2012, ⟨10.1002/9783527644506.ch21⟩. ⟨hal-00809254⟩
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