Protein folding from a highly disordered denatured state: The folding pathway of chymotrypsin inhibitor 2 at atomic resolution
Open Access
- 27 March 2001
- journal article
- Published by Proceedings of the National Academy of Sciences in Proceedings of the National Academy of Sciences
- Vol. 98 (8) , 4349-4354
- https://doi.org/10.1073/pnas.071054398
Abstract
Previous experimental and theoretical studies have produced high-resolution descriptions of the native and folding transition states of chymotrypsin inhibitor 2 (CI2). In similar fashion, here we use a combination of NMR experiments and molecular dynamics simulations to examine the conformations populated by CI2 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.Keywords
This publication has 32 references indexed in Scilit:
- Towards a complete description of the structural and dynamic properties of the denatured state of barnase and the role of residual structure in folding 1 1Edited by B. HonigJournal of Molecular Biology, 2000
- "New View" of Protein Folding Reconciled with the Old Through Multiple Unfolding SimulationsScience, 1997
- Following co-operative formation of secondary and tertiary structure in a single protein moduleJournal of Molecular Biology, 1997
- Identification and Characterization of the Unfolding Transition State of Chymotrypsin Inhibitor 2 by Molecular Dynamics SimulationsJournal of Molecular Biology, 1996
- Structure of the Transition State for Folding of a Protein Derived from Experiment and SimulationJournal of Molecular Biology, 1996
- Perturbed pKA-values in the Denatured States of ProteinsJournal of Molecular Biology, 1995
- The structure of the transition state for the association of two fragments of the barley chymotrypsin inhibitor 2 to generate native-like protein: implications for mechanisms of protein folding.Proceedings of the National Academy of Sciences, 1994
- Characterization of the transition state of protein unfolding by use of molecular dynamics: chymotrypsin inhibitor 2.Proceedings of the National Academy of Sciences, 1994
- Structure of the transition state for the folding/unfolding of the barley chymotrypsin inhibitor 2 and its implications for mechanisms of protein folding.Proceedings of the National Academy of Sciences, 1994
- Mapping the transition state and pathway of protein folding by protein engineeringNature, 1989