Protein Folding Triggered by Electron Transfer

Proteins do not fold by randomly searching a large of nearly degenerate configurations; instead, an of unfolded molecules must traverse a complicated landscape to reach a thermodynamically stable structure. The fastest nuclear motions in proteins, about single bonds, occur on the picosecond scale and accompany both secondary- and -structure-forming processes. Short segments of structure (e.g., α-helices) can be formed in , whereas the large-scale, collective motions with the development of tertiary structure fall the microsecond to millisecond range. Misfolded or traps are frequently encountered in folding ; escape from these traps (e.g., proline isomerization) can take seconds or even minutes. Understanding the key events in folding and identifying any partially folded intermediates are major goals of theoretical and experimental work.