The relation among thermodynamic stability, folding dynamics, and designability

Citation
R. Tatsumi et al., The relation among thermodynamic stability, folding dynamics, and designability, PROG T PH S, (138), 2000, pp. 420-421
Citations number
11
Categorie Soggetti
Physics
Journal title
PROGRESS OF THEORETICAL PHYSICS SUPPLEMENT
ISSN journal
03759687 → ACNP
Issue
138
Year of publication
2000
Pages
420 - 421
Database
ISI
SICI code
0375-9687(2000):138<420:TRATSF>2.0.ZU;2-U
Abstract
We examined the relation among thermodynamic stability, folding rates, and designability at lattice proteins. We found no clear correlations among the se three conditions. This implies that sequences having highly designable s tructure as native slate do not necessarily satisfy both high thermodynamic stability and fast folding property. This conclusion may apply to natural proteins belonging to the same superfamily or superfold.