Universal model for α-helix and β-sheet structures in protein

Jeff Z.Y. Chen and Hideo Imamura

Physica A: Statistical Mechanics and its Applications, 2003, vol. 321, issue 1, 181-188

Abstract: We present a unified potential-energy model that successfully reproduces the hydrogen bonding effect in proteins and can be used to represent well-defined secondary structures, both α-helices and β-sheets. The native structures of the model contain both α-helices and β-sheets and are entirely dependent on the sequence of the modelled protein. The model provides structural insight into the physical mechanism of such problems as structural conversion due to mutation and double native conformations with different α-helix and β-sheet contents.

Keywords: Protein secondary structures; Alpha helix; Beta sheet; Structural formation; Structural transition (search for similar items in EconPapers)
Date: 2003
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Persistent link: https://EconPapers.repec.org/RePEc:eee:phsmap:v:321:y:2003:i:1:p:181-188

DOI: 10.1016/S0378-4371(02)01789-2

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