title
  

Relaxation kinetics and the glassiness of native proteins: coupling of timescales

Warning The system is temporarily closed to updates for reporting purpose.

Baysal, Canan and Atılgan, Ali Rana (2005) Relaxation kinetics and the glassiness of native proteins: coupling of timescales. Biophysical Journal, 88 (3). pp. 1570-1576. ISSN 0006-3495 (Print) 1542-0086 (Online)

[img]
Preview
PDF (Open Access) - Requires a PDF viewer such as GSview, Xpdf or Adobe Acrobat Reader
134Kb

Official URL: http://dx.doi.org/10.1529/biophysj.104.050252

Abstract

We provide evidence that the onset of functional dynamics of folded proteins with elevated temperatures is associated with the effective sampling of its energy landscape under physiological conditions. The analysis is based on data describing the relaxation phenomena governing the backbone dynamics of bovine pancreatic trypsin inhibitor derived from molecular dynamics simulations, previously reported by us. By representing the backbone dynamics of the folded protein by three distinct regimes, it is possible to decompose its seemingly complex dynamics, described by a stretch exponential decay of the backbone motions. Of these three regimes, one is associated with the slow timescales due to the activity along the envelope of the energy surface defining the folded protein. Another, with fast timescales, is due to the activity along the pockets decorating the folded-state envelope. The intermediate regime emerges at temperatures where jumps between the pockets become possible. It is at the temperature window where motions corresponding to all three timescales become operative that the protein becomes active.

Item Type:Article
Additional Information:WoS - Open Access (Green Published) / Scopus - Open Access
Subjects:Q Science > QP Physiology
ID Code:368
Deposited By:Canan Atılgan
Deposited On:16 Feb 2007 02:00
Last Modified:23 Jul 2020 16:36

Repository Staff Only: item control page