title: Methanol strengthens hydrogen bonds and weakens hydrophobic interactions in proteins--a combined molecular dynamics and NMR study.
abstract: A combined simulation and experimental study was performed to investigate how methanol affects the structure of a model peptide BBA5. BBA5 forms a stable β-hairpin-α-helix structure in aqueous solutions. Molecular dynamics simulations were performed in water and methanol/water solutions using all-atom explicit models. NMR experiments were used to test the calculated results. The combined theoretical and experimental studies suggest that methanol strengthens the interactions between the polar backbone of the peptide and thus enhances the secondary structure formation; at the same time methanol weakens the hydrophobic interactions and results in an expansion of the hydrophobic core and an increase in gyration.
authors.affiliation: Center for Biological NMR, Department of Chemistry, Texas A&M University, College Station, Texas 77843, United States.
authors.forename: Soyoun
authors.initials: S
authors.lastname: Hwang
authors.forename: Qiang
authors.initials: Q
authors.lastname: Shao
authors.forename: Howard
authors.initials: H
authors.lastname: Williams
authors.forename: Christian
authors.initials: C
authors.lastname: Hilty
authors.forename: Yi Qin
authors.initials: YQ
authors.lastname: Gao
mesh_terms: D000595:Amino Acid Sequence; D006860:Hydrogen Bonding; D057927:Hydrophobic and Hydrophilic Interactions; D000432:Methanol / Q000737:chemistry*; D056004:Molecular Dynamics Simulation; D008969:Molecular Sequence Data; D019906:Nuclear Magnetic Resonance, Biomolecular; D010455:Peptides / Q000737:chemistry*; D017433:Protein Structure, Secondary
chemical_list: D010455:Peptides; D000432:Methanol