Abstract
The mechanism of β-sheet cooperativity without side-chain interactions, at the different choice of the H-bond potential, was explored. The results indicate that in the absence of hydrophobic clustering, the β-sheet cooperativity arises from a combination of structural factors, protein de/solvation effects, and the system topology.
Original language | English |
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Pages (from-to) | 4353-4365 |
Number of pages | 13 |
Journal | Journal of Chemical Physics |
Volume | 116 |
Issue number | 10 |
DOIs | |
State | Published - 8 Mar 2002 |