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Temperature dependence of normal mode reconstructions of protein dynamics (Articolo in rivista)

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Temperature dependence of normal mode reconstructions of protein dynamics (Articolo in rivista) (literal)

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Alternative label

Piazza F. (1), De Los Rios P. (1) , Cecconi F. (2) (2009)
Temperature dependence of normal mode reconstructions of protein dynamics
in Physical review letters (Print); The American Physical Society, College Park, MD 20740-3844 (Stati Uniti d'America)
(literal)

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1) Laboratoire de Biophysique Statistique, SB ITP, Ecole Polytechnique Fédérale de Lausanne - EPFL, CH-1015, Lausanne, Switzerland 2) SMC-INFM Center for Statistical Mechanics and Complexity (CNR) and Istituto dei Sistemi Complessi CNR, Via dei Taurini 19, 00185 Rome, Italy (literal)

Titolo

Temperature dependence of normal mode reconstructions of protein dynamics (literal)

Abstract

Normal mode (NM) analysis is a widely used technique for reconstructing conformational changes of proteins from the knowledge of native structures. In this Letter, we investigate to what extent NMs capture the salient features of the dynamics over a range of temperatures from close to T=0 to above unfolding. We show that the use of normal modes at room temperature is justified provided proteins are cooperative, that is, globular and highly structured. On the other hand, it is imperative to consider several modes in order to eliminate the unpredictable temperature dependence of single-mode contributions to the protein fluctuations. (literal)

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