Bethe approximation for the hydrogen-bonding self-avoiding walk in a solvent
D. P. Foster, M. Aniambossou
TL;DR
This paper investigates a square-lattice model for protein secondary structures, incorporating hydrogen bonding and solvent effects, analyzed using the Bethe approximation to understand their interplay.
Contribution
It extends the hydrogen-bonding self-avoiding walk model by including solvent quality effects within the Bethe approximation framework.
Findings
Insights into how solvent quality influences hydrogen-bonding in protein models
Application of Bethe approximation to complex lattice models of proteins
Potential implications for understanding protein folding mechanisms
Abstract
A square-lattice model for the formation of secondary structures in proteins, the hydrogen-bonding model, extended to include the effects of solvent quality, is examined in the framework of the Bethe approximation.
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Taxonomy
TopicsProtein Structure and Dynamics · Molecular spectroscopy and chirality · Crystallography and molecular interactions