Direct observation of hierarchical protein dynamics-Reference-Cited by-同舟云学术

Direct observation of hierarchical protein dynamics

Published:2015-05 Issue:6234 Volume:348 Page:578-581
ISSN:0036-8075
Container-title:Science
language:en
Short-container-title:Science

Author:

Lewandowski Józef R.¹,Halse Meghan E.¹,Blackledge Martin²,Emsley Lyndon¹³

Affiliation:

1. Université de Lyon, Institut de Sciences Analytiques (CNRS/ENS-Lyon/UCB-Lyon 1), Centre de Résonance Magnétique Nucléaire à Très Hauts Champs, 69100 Villeurbanne, France.

2. Université Grenoble Alpes, Institut de Biologie Structurale (IBS), F-38044 Grenoble, France; CNRS, IBS, F-38044 Grenoble, France; CEA, IBS, F-38044 Grenoble, France.

3. Institut des Sciences et Ingénierie Chimiques, Ecole Polytechnique Fédérale de Lausanne (EPFL), CH-1015 Lausanne, Switzerland.

Abstract

A hierarchy of protein motions Functioning proteins are not static but explore complex conformational energy landscapes. Lewandowski et al. used multinuclear solid-state nuclear magnetic resonance experiments to measure protein motion over a broad range of temperatures and time scales. Above 160 K there was a strong coupling between solvent and protein motion. The hierarchy of motions as the temperature increased revealed the dynamic modes that relate solvent, sidechain, and backbone motion. Science , this issue p. 578

Funder

Seventh Framework Program of the European Commission

Agence Nationale de la Recherche

Swiss National Science Foundation

European Union International Reintegration

Publisher

American Association for the Advancement of Science (AAAS)

Subject

Multidisciplinary

Reference79 articles.

1. The Energy Landscapes and Motions of Proteins

2. Crystalline ribonuclease A loses function below the dynamical transition at 220 K