Article
Nonnative interactions in the FF domain folding pathway from an atomic resolution structure of a sparsely populated intermediate: an NMR relaxation dispersion study.
Journal of the American Chemical Society - 20 Jul 2011
Korzhnev Dmitry M, Vernon Robert M, Religa Tomasz L, Hansen Alexandar L, Baker David, Fersht Alan R, Kay Lewis E
Abstract excerpt
Several all-helical single-domain proteins have been shown to fold rapidly (microsecond time scale) to a compact intermediate state and subsequently rearrange more slowly to the native conformation. An understanding of this process has been hindered by difficulties in experimental studies of intermediates in cases where they are both low-populated and only transiently formed. One such example is provided by the...
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