5 Papers
46 Citations
Rui Zhou is an academic researcher from Huazhong University of Science and Technology. The author has contributed to research in topics: Phi value analysis & Protein folding. The author has an hindex of 3, co-authored 5 publications.
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Papers
Folding kinetics of WW domains with the united residue force field for bridging microscopic motions and experimental measurements.
Rui Zhou,Gia G. Maisuradze,David Suñol,Toni Todorovski,Maria J. Macias,Yi Xiao,Harold A. Scheraga,Cezary Czaplewski,Adam Liwo +8 more
TL;DR: The results indicate that the UNRES force field can provide accurate predictions of folding kinetics of these WW domains, often used as models for the study of the mechanisms of proein folding.
Effects of mutation, truncation, and temperature on the folding kinetics of a WW domain.
TL;DR: Three-state folding is found to be a main mechanism for folding the FBP28 WW domain and most of the full-size and truncated mutants.
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Brief Communication: Foldable subunits of helix protein
TL;DR: This work simulated the folding of a six-helix protein with a length of 120 amino acids and found that its two halves can fold into native conformations independently, suggesting that this protein may be divided into two foldable halves.
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STUDY OF FOLDING BEHAVIORS OF A SIX-HELIX PROTEIN BY ab initio MOLECULAR DYNAMICS FOLDING SIMULATIONS OF UNRES
TL;DR: In this article, the authors employ United-Residue (UNRES) approach to study folding processes of a six-helix protein domain (the C-terminal domain of Ku86 protein, PDB ID: 1Q2Z).
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Multi-nucleation and vectorial folding pathways of large helix protein
TL;DR: It is found that all three-helix subunits in the chain can fold into native-like conformations independently, especially those at the two terminal parts and the middle of the chain, which may be responsible for the nucleation's.
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