title: Adherence of packing defects in soluble proteins.
abstract: For protein structure to prevail in water, its backbone hydrogen bonds must be shielded from water attack, requiring a cluster of "wrapping" nonpolar groups. Thus, underwrapped regions are adhesive, as exogenous removal of surrounding water becomes thermodynamically favorable. Here we measure the average adhesive force exerted by an underwrapped hydrogen bond on a test hydrophobe and thus define a new interactivity constant.
authors.affiliation: Institute for Biophysical Dynamics, The University of Chicago, Chicago, Illinois 60637, USA. ariel@uchicago.edu
authors.forename: Ariel
authors.initials: A
authors.lastname: Fernández
authors.forename: L Ridgway
authors.initials: LR
authors.lastname: Scott
mesh_terms: D001059:Apoproteins / Q000737:chemistry; D006801:Humans; D006860:Hydrogen Bonding; D057927:Hydrophobic and Hydrophilic Interactions; D008956:Models, Chemical; D009113:Muramidase / Q000737:chemistry; D009211:Myoglobin / Q000737:chemistry; D011487:Protein Conformation; D011506:Proteins / Q000737:chemistry*; D012995:Solubility; D014867:Water / Q000737:chemistry; D001613:beta 2-Microglobulin / Q000737:chemistry
chemical_list: D001059:Apoproteins; D009211:Myoglobin; D011506:Proteins; C010857:apomyoglobin; D001613:beta 2-Microglobulin; D014867:Water; D009113:Muramidase