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Molecular modeling of hair keratin/peptide complex: Using MM‐PBSA calculations to describe experimental binding results
Author(s) -
Azoia Nuno G.,
Fernandes Margarida M.,
Micaêlo Nuno M.,
Soares Cláudio M.,
CavacoPaulo Artur
Publication year - 2012
Publication title -
proteins: structure, function, and bioinformatics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.699
H-Index - 191
eISSN - 1097-0134
pISSN - 0887-3585
DOI - 10.1002/prot.24037
Subject(s) - keratin , peptide , computational biology , molecular dynamics , chemistry , molecular model , biophysics , biochemistry , computational chemistry , biology , genetics
Molecular dynamics simulations of a keratin/peptide complex have been conducted to predict the binding affinity of four different peptides toward human hair. Free energy calculations on the peptides' interaction with the keratin model demonstrated that electrostatic interactions are believed to be the main driving force stabilizing the complex. The molecular mechanics–Poisson‐Boltzmann surface area methodology used for the free energy calculations demonstrated that the dielectric constant in the protein's interior plays a major role in the free energy calculations, and the only way to obtain accordance between the free energy calculations and the experimental binding results was to use the average dielectric constant. Proteins 2012;. © 2012 Wiley Periodicals, Inc.