Desolvation shell of hydrogen bonds in folded proteins, protein complexes and folding pathways.
A few backbone hydrogen bonds (HBS) in native protein folds are poorly protected from water attack: their desolvation shell contains an inordinately low number of hydrophobic residues. Thus, an approach by solvent-structuring moieties of a binding partner should contribute significantly to enhance their stability. This effect represents an important factor in the site specificity inherent to protein binding, as inferred from a strong correlation between poorly desolvated HBs and binding sites. The desolvation shells were also examined in a dynamic context: except for a few singular under-protected bonds, the size of desolvation shells is preserved along the folding trajectory.
Fernández
Ariel
A
Institute for Biophysical Dynamics, Cummings Life Science Center #439D, The University of Chicago, 920 East 58th Street, Chicago, IL 60637, USA. ariel@uchicago.edu
D006860:Hydrogen Bonding; D008958:Models, Molecular; D011485:Protein Binding; D017510:Protein Folding; D011506:Proteins / Q000737:chemistry* / Q000378:metabolism; D012997:Solvents / Q000737:chemistry
D011506:Proteins; D012997:Solvents