Machinery of Functional Dynamics in Native Proteins

Thumbnail Image

Date

Authors

Journal Title

Journal ISSN

Volume Title

Publisher

Abstract

Description

We provide evidence that the energy landscapes of folded proteins do not shift with temperature, but the onset of functional dynamics is associated with its effective sampling. The motion of the backbone is described by three distinct regimes. One is associated with slow time scales of the activity along the envelope of the energy surface defining the folded protein. Another, with fast time scales, is due to activity along the pockets decorating the folded-state envelope. The intermediate regime emerges at temperatures where jumps between the pockets become possible, leading to an active protein.
13 pages with 4 figures; submitted to Phys. Rev. Lett

Keywords

Soft Condensed Matter, Biomolecules

Citation

URI

http://salesiana.dossiersoluciones.com/handle/123456789/22257

Consulte el texto completo en el siguiente enlace:

https://arxiv.org/abs/cond-mat/0309448
 http://arxiv.org/abs/cond-mat/0309448

Collections

arXiv