Cooperative sub-millisecond folding kinetics of apomyoglobin pH 4 intermediate.

Abstract

For small single-domain proteins, formation of the native conformation (N) from a fully unfolded form (U) or from a partially folded intermediate (I) occurs typically in a highly cooperative process that can be described by a two-state model. However, it is not clear whether cooperativity arises early along the folding reaction and whether folding… (More)

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@article{Weisbuch2005CooperativeSF, title={Cooperative sub-millisecond folding kinetics of apomyoglobin pH 4 intermediate.}, author={S{\'e}bastien Weisbuch and Francine C. A. G{\'e}rard and Marielle Pasdeloup and J{\'e}remy Cappadoro and Yves Dupont and Marc Jamin}, journal={Biochemistry}, year={2005}, volume={44 18}, pages={7013-23} }