Abstract
Protein folding is modeled as diffusion on a free-energy landscape, allowing use of the diffusion equation to study the impact of energetic parameters on the folding dynamics. The free-energy landscape is characterized by two different order parameters, one representing the degree of compactness, the other a measure of the progress towards the folded state. For marginally stable proteins, fastest folding is achieved when the nonspecific interactions favoring compaction are strong, resulting in a high folding temperature. Such proteins fold by rapid collapse followed by slower accumulation of correct contacts.
Original language | English (US) |
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Pages (from-to) | 4408-4415 |
Number of pages | 8 |
Journal | Journal of Chemical Physics |
Volume | 107 |
Issue number | 11 |
DOIs | |
State | Published - Sep 18 1997 |