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

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.

journal_name

Biophys J

journal_title

Biophysical journal

authors

Baysal C,Atilgan AR

doi

10.1529/biophysj.104.050252

subject

Has Abstract

pub_date

2005-03-01 00:00:00

pages

1570-6

issue

3

eissn

0006-3495

issn

1542-0086

pii

S0006-3495(05)73224-0

journal_volume

88

pub_type

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