title: Relationship between intramolecular hydrogen bonding and solvent accessibility of side-chain donors and acceptors in proteins.
abstract: 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.
authors: Institute of Protein Research, Russian Academy of Sciences, 142290 Moscow Region, Pushchino, Russia. efimov@protres.ru
authors: Alexander V
authors: AV
authors: Efimov
authors: Evgenii V
authors: EV
authors: Brazhnikov
mesh_terms: D000596:Amino Acids / Q000737:chemistry*; D018360:Crystallography, X-Ray; D006860:Hydrogen Bonding; D009584:Nitrogen / Q000737:chemistry; D010100:Oxygen / Q000737:chemistry; D011506:Proteins / Q000737:chemistry*; D012997:Solvents / Q000737:chemistry*; D013816:Thermodynamics; D014867:Water / Q000737:chemistry
chemical_list: D000596:Amino Acids; D011506:Proteins; D012997:Solvents; D014867:Water; D009584:Nitrogen; D010100:Oxygen