Sequence rotation in N-dimensional space and the folding of hydrophobic protein models: Surpassing the diagonal unfolded state approximation
Author:
Publisher
AIP Publishing
Subject
Physical and Theoretical Chemistry,General Physics and Astronomy
Reference45 articles.
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1. Native atomic burials, supplemented by physically motivated hydrogen bond constraints, contain sufficient information to determine the tertiary structure of small globular proteins;Proteins: Structure, Function, and Bioinformatics;2008-01-02
2. Description of atomic burials in compact globular proteins by Fermi-Dirac probability distributions;Proteins: Structure, Function, and Bioinformatics;2006-11-15
3. Folding pathway dependence on energetic frustration and interaction heterogeneity for a three-dimensional hydrophobic protein model;Proteins: Structure, Function, and Bioinformatics;2005-11-16
4. Entropy reduction effect imposed by hydrogen bond formation on protein folding cooperativity: Evidence from a hydrophobic minimalist model;Physical Review E;2005-11-01
5. Imaging Proteins with Atomic Force Microscopy: An Overview;Current Protein & Peptide Science;2005-08-01
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