Journal
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
Volume 98, Issue 8, Pages 4349-4354Publisher
NATL ACAD SCIENCES
DOI: 10.1073/pnas.071054398
Keywords
CI2; nuclear magnetic resonance; molecular dynamics simulations; conformational transitions; nucleation-condensation
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Funding
- NIGMS NIH HHS [T32 GM008268, GM 50789, GM 08268, R29 GM050789, R01 GM050789] Funding Source: Medline
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Previous experimental and theoretical studies have produced high-resolution descriptions of the native and folding transition states of chymotrypsin inhibitor 2 (C12), In similar fashion, here we use a combination of NMR experiments and molecular dynamics simulations to examine the conformations populated by C12 in the denatured state, The denatured state is highly unfolded, but there is some residual native helical structure along with hydrophobic clustering in the center of the chain. The lack of persistent nonnative structure in the denatured state reduces barriers that must be overcome, leading to fast folding through a nucleation-condensation mechanism. With the characterization of the denatured state, we have now completed our description of the folding/unfolding pathway of CI2 at atomic resolution.
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