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Desolvation shell of hydrogen bonds in folded proteins, protein complexes and folding pathways
Author(s) -
Fernández Ariel
Publication year - 2002
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(02)03204-0
Subject(s) - hydrogen bond , folding (dsp implementation) , chemistry , context (archaeology) , protein folding , crystallography , shell (structure) , hydrophobic effect , solvation shell , solvent , biochemistry , molecule , organic chemistry , materials science , solvation , biology , paleontology , electrical engineering , composite material , engineering
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.