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Int. J. Mol. Sci. 2009, 10(6), 2838-2848; doi:10.3390/ijms10062838
Review

Folding Mechanism of Beta-Hairpin Trpzip2: Heterogeneity, Transition State and Folding Pathways

* ,
 and
Biomolecular Physics and Modeling Group, Department of Physics, Huazhong University of Science and Technology, Wuhan 430074, Hubei, China
* Author to whom correspondence should be addressed.
Received: 26 May 2009 / Revised: 18 June 2009 / Accepted: 19 June 2009 / Published: 22 June 2009
(This article belongs to the Special Issue Protein Folding)
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Abstract

We review the studies on the folding mechanism of the β-hairpin tryptophan zipper 2 (trpzip2) and present some additional computational results to refine the picture of folding heterogeneity and pathways. We show that trpzip2 can have a two-state or a multi-state folding pattern, depending on whether it folds within the native basin or through local state basins on the high-dimensional free energy surface; Trpzip2 can fold along different pathways according to the packing order of tryptophan pairs. We also point out some important problems related to the folding mechanism of trpzip2 that still need clarification, e.g., a wide distribution of the computed conformations for the transition state ensemble.
Keywords: beta-hairpin; trpzip2; folding heterogeneity; transition state; folding pathway beta-hairpin; trpzip2; folding heterogeneity; transition state; folding pathway
This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.

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Xiao, Y.; Chen, C.; He, Y. Folding Mechanism of Beta-Hairpin Trpzip2: Heterogeneity, Transition State and Folding Pathways. Int. J. Mol. Sci. 2009, 10, 2838-2848.

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