Sl. Kazmirski et al., Protein folding from a highly disordered denatured state: The folding pathway of chymotrypsin inhibitor 2 at atomic resolution, P NAS US, 98(8), 2001, pp. 4349-4354
Citations number
36
Categorie Soggetti
Multidisciplinary
Journal title
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
Previous experimental and theoretical studies have produced high-resolution
descriptions of the native and folding transition states of chymotrypsin i
nhibitor 2 (C12), In similar fashion, here we use a combination of NMR expe
riments and molecular dynamics simulations to examine the conformations pop
ulated by C12 in the denatured state, The denatured state is highly unfolde
d, but there is some residual native helical structure along with hydrophob
ic clustering in the center of the chain. The lack of persistent nonnative
structure in the denatured state reduces barriers that must be overcome, le
ading to fast folding through a nucleation-condensation mechanism. With the
characterization of the denatured state, we have now completed our descrip
tion of the folding/unfolding pathway of CI2 at atomic resolution.