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Studies of protein hydration in aqueous solution by high‐resolution nuclear magnetic resonance spectroscopy
Author(s) -
Wüthrich Kurt,
Otting Gottfried
Publication year - 1992
Publication title -
international journal of quantum chemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.484
H-Index - 105
eISSN - 1097-461X
pISSN - 0020-7608
DOI - 10.1002/qua.560420528
Subject(s) - chemistry , homonuclear molecule , heteronuclear molecule , aqueous solution , molecule , water of crystallization , nuclear magnetic resonance spectroscopy , nuclear overhauser effect , crystallography , hydrogen bond , solvent , two dimensional nuclear magnetic resonance spectroscopy , inorganic chemistry , stereochemistry , organic chemistry
Individual hydration water molecules in aqueous protein solutions have been observed using experimental schemes for homonuclear two‐dimensional and heteronuclear three‐dimensional NMR experiments in H 2 O solution, which do not require suppression of the solvent line by presaturation. In these experiments, the location of the hydration waters is determined from their nuclear Overhauser effects ( NOE s) with individual hydrogen atoms of distinct amino acid residues. In the basic pancreatic trypsin inhibitor ( BPTI ), four internal water molecules that had been reported in three different crystal forms were also found to be in the same locations in the solution structure, with lifetimes with respect to exchange of the water protons in excess of 0.3 ns. Additional NOE s with polypeptide protons located on the protein surface may involve either hydration water molecules or hydroxyl protons of amino acid side chains. Their total number is small compared to the number of NOE s expected from the hydration water molecules identified in the crystal structures of BPTI .