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Updated: Aug 30, 2026

Analyzing Protein Dynamics Using Hydrogen Exchange Mass Spectrometry
Published on: November 29, 2013
Relationship between intramolecular hydrogen bonding and solvent accessibility of side-chain donors and acceptors in
Alexander V Efimov1, Evgenii V Brazhnikov
1Institute of Protein Research, Russian Academy of Sciences, 142290 Moscow Region, Pushchino, Russia. efimov@protres.ru
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.
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