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Relationship between intramolecular hydrogen bonding and solvent accessibility of side‐chain donors and acceptors in proteins
Author(s) -
Efimov Alexander V,
Brazhnikov Evgenii V
Publication year - 2003
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(03)01189-x
Subject(s) - intramolecular force , hydrogen bond , solvent , chemistry , acceptor , molecule , side chain , photochemistry , crystallography , stereochemistry , organic chemistry , polymer , physics , condensed matter physics
This study shows that intramolecular hydrogen bonding in proteins depends on the accessibility of donors and acceptors to water molecules. The frequency of occurrence of H‐bonded side chains in proteins is inversely proportional to the solvent accessibility of their donors and acceptors. Estimates of the notional free energy of hydrogen bonding suggest that intramolecular hydrogen‐bonding interactions of buried and half‐buried donors and acceptors can contribute favorably to the stability of a protein, whereas those of solvent‐exposed polar atoms become less favorable or unfavorable.