ReviewInternational journal of molecular sciences2009
Folding mechanism of β-hairpin trpzip2: heterogeneity, transition state and folding pathways.
Review in International journal of molecular sciences, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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Who cites it
6 citing papers in PubMed.
- A Structure Independent Molecular Fragment Interfuse Model for Mesoscale Dissipative Particle Dynamics Simulation of Peptides.ACS omega · 2024Article
- Granger Causality Analysis of Chignolin Folding.Journal of chemical theory and computation · 2022Article
- A cellular chemical probe targeting the chromodomains of Polycomb repressive complex 1.Nature chemical biology · 2016Article
- Correct folding of an α-helix and a β-hairpin using a polarized 2D torsional potential.Scientific reports · 2015Article
- Infrared study of the stability and folding kinetics of a series of β-hairpin peptides with a common NPDG turn.The journal of physical chemistry. B · 2011Article
- Stability and folding behavior analysis of zinc-finger using simple models.International journal of molecular sciences · 2010Article
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Authors and funding
3 authors.
Funding
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Abstract
We review the studies on the folding mechanism of the beta-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.
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