Adherence of packing defects in soluble proteins.
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.
Fernández
Ariel
A
Institute for Biophysical Dynamics, The University of Chicago, Chicago, Illinois 60637, USA. ariel@uchicago.edu
Scott
L Ridgway
LR
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
D001059:Apoproteins; D009211:Myoglobin; D011506:Proteins; C010857:apomyoglobin; D001613:beta 2-Microglobulin; D014867:Water; D009113:Muramidase