Folding of proteins in presculpted free energy landscape

Nguyen Ba Hung, Trinh Xuan Hoang
Author affiliations

Authors

  • Nguyen Ba Hung Vietnam Military Medical University, 104 Phung Hung, Ha Dong, Hanoi, Vietnam
  • Trinh Xuan Hoang Institute of Physics, Vietnam Academy of Science and Technology

DOI:

https://doi.org/10.15625/0868-3166/23/4/3091

Keywords:

protein folding, tube model, Go model, Monte Carlo simulation

Abstract

Recent studies of the tube model of protein have indicated that the free energy landscape of proteins is presculpted by symmetry of the protein backbone and geometrical constraints played by the hydrogen bonds. In this study, we investigate the role of amino acid sequences in the folding of proteins. We consider two models that are differed by sequence specificity: the tube HP model with hydrophobic (H) and polar (P) sequences, and the tube Go model with native-centric contact potentials. Monte Carlo simulations are carried out for two sequences of length of 48 amino acids, whose ground states are a three-helix bundle and a GB1-like structure.  The results show that folding inthe Go model is more cooperative than in the HP model. In the HP model the collapse transition and the folding transition are separated, whereas in the Go model the two transitions coincide.

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Published

26-09-2013

How to Cite

[1]
N. B. Hung and T. X. Hoang, “Folding of proteins in presculpted free energy landscape”, Comm. Phys., vol. 23, no. 4, p. 313, Sep. 2013.

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Papers
Received 09-07-2013
Published 26-09-2013