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 Jjournal_title
Biophysical journalauthors
Baysal C,Atilgan ARdoi
10.1529/biophysj.104.050252subject
Has Abstractpub_date
2005-03-01 00:00:00pages
1570-6issue
3eissn
0006-3495issn
1542-0086pii
S0006-3495(05)73224-0journal_volume
88pub_type
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