title: Buffering the entropic cost of hydrophobic collapse in protein chains.
abstract: Direct inspection of high-resolution protein structures reveals that backbone dehydration promotes extra conformational freedom in the peptide bond, especially when the residue is not involved in secondary structure. The results imply a buffering effect that lowers the entropic cost of hydrophobic collapse. (c) 2004 American Institute of Physics.
authors.forename: Ariel
authors.initials: A
authors.lastname: Fernández
mesh_terms: D001703:Biophysics / Q000379:methods*; D030562:Databases, Protein; D019277:Entropy; D006860:Hydrogen Bonding; D010455:Peptides / Q000737:chemistry; D011487:Protein Conformation; D017510:Protein Folding; D017433:Protein Structure, Secondary; D011506:Proteins / Q000737:chemistry*
chemical_list: D010455:Peptides; D011506:Proteins