Three-helix-bundle Protein in a Ramachandran Model

Details Three-helix-bundle Protein in a Ramachandran Model Three-helix-bundle Protein in a Ramachandran Model

2000-11-05

arxiv.org/abs/cond-mat/0011079v1

Proc. Natl. Acad. Sci. USA 97 (2000) 13614-13618

Physics

Condensed Matter

Soft Condensed Matter

15 pages, 7 figures

Scientific paper

10.1073/pnas.240245297

We study the thermodynamic behavior of a model protein with 54 amino acids that forms a three-helix bundle in its native state. The model contains three types of amino acids and five to six atoms per amino acid and has the Ramachandran torsional angles $\phi_i$, $\psi_i$ as its degrees of freedom. The force field is based on hydrogen bonds and effective hydrophobicity forces. For a suitable choice of the relative strength of these interactions, we find that the three-helix-bundle protein undergoes an abrupt folding transition from an expanded state to the native state. Also shown is that the corresponding one- and two-helix segments are less stable than the three-helix sequence.

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