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FEBS Lett ; 554(3): 389-93, 2003 Nov 20.
Article in English | MEDLINE | ID: mdl-14623099

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.


Subject(s)
Amino Acids/chemistry , Proteins/chemistry , Solvents/chemistry , Crystallography, X-Ray , Hydrogen Bonding , Nitrogen/chemistry , Oxygen/chemistry , Thermodynamics , Water/chemistry
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