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© Research
Publication : PURE AND APPLIED CHEMISTRY

Nuclear magnetic resonance as a quantitative tool to study interactions in biomacromolecules

Scientific Fields
Diseases
Organisms
Applications
Technique

Published in PURE AND APPLIED CHEMISTRY - 01 Aug 2005

Grzesiek, S; Allan, M; Cordier, F; Haussinger, D; Jensen, P; Kahmann, J; Meier, S; Sass, HJ

PURE AND APPLIED CHEMISTRY 2005; 77(8): 1409-1424

High-resolution nuclear magnetic resonance (NMR) has emerged as one of the most versatile tools for the quantitative study of structure, kinetics, and thermodynamics of biomolecules and their interactions at atomic resolution. Traditionally, nuclear Overhauser enhancements (NOEs) and chemical shift perturbation methods are used to determine molecular geometries and to identify contact surfaces, but more recently, weak anisotropic orientation, anisotropic diffusion, and scalar couplings across hydrogen bonds provide additional information.

Examples of such technologies are shown as applied to the quantitative characterization of function and thermodynamics of several biomacromolecules. In particular, (1) the structural and dynamical changes of the TipA multidrug resistance protein are followed upon antibiotic binding, (2) the trimer-monomer equilibrium and thermal unfolding of foldon, a small and very efficient trimerization domain of the 14 phagehead, is described in atomic detail, and (3) the changes of individual protein hydrogen bonds during thermal unfolding are quantitatively followed by scalar couplings across hydrogen bonds.