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Acid–base chemistry of frustrated water at protein interfaces
Author(s) -
Fernández Ariel
Publication year - 2016
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 - 10.1002/1873-3468.12047
Subject(s) - hydronium , frustration , chemistry , hydrogen bond , proton , ammonium , aqueous solution , crystallography , molecule , base (topology) , quantum chemistry , charge (physics) , chemical physics , inorganic chemistry , crystal structure , organic chemistry , supramolecular chemistry , physics , condensed matter physics , quantum mechanics , mathematical analysis , mathematics
Water molecules at a protein interface are often frustrated in hydrogen‐bonding opportunities due to subnanoscale confinement. As shown, this condition makes them behave as a general base that may titrate side‐chain ammonium and guanidinium cations. Frustration‐based chemistry is captured by a quantum mechanical treatment of proton transference and shown to remove same‐charge uncompensated anticontacts at the interface found in the crystallographic record and in other spectroscopic information on the aqueous interface. Such observations are untenable within classical arguments, as hydronium is a stronger acid than ammonium or guanidinium. Frustration enables a directed Grotthuss mechanism for proton transference stabilizing same‐charge anticontacts.