Machinery of Functional Dynamics in Native Proteins

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dc.creatorBaysal, Canan
dc.creatorAtilgan, Ali Rana
dc.date2003-09-19
dc.date.accessioned2026-07-07T02:53:33Z
dc.date.available2026-07-07T02:53:33Z
dc.descriptionWe 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.
dc.description13 pages with 4 figures; submitted to Phys. Rev. Lett
dc.identifierhttps://arxiv.org/abs/cond-mat/0309448
dc.identifierhttp://arxiv.org/abs/cond-mat/0309448
dc.identifier.urihttp://salesiana.dossiersoluciones.com/handle/123456789/22257
dc.subjectSoft Condensed Matter
dc.subjectBiomolecules
dc.titleMachinery of Functional Dynamics in Native Proteins
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