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Influence of thermal motion on 1 H chemical shifts in proteins: the case of bovine pancreatic trypsin inhibitor
Author(s) -
Busetta Bernard,
Picard Philippe,
Precigoux Gilles
Publication year - 2001
Publication title -
journal of peptide science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.475
H-Index - 66
eISSN - 1099-1387
pISSN - 1075-2617
DOI - 10.1002/psc.300
Subject(s) - chemistry , chemical shift , hydrogen bond , thermal motion , trypsin , proton , side chain , peptide bond , trypsin inhibitor , thermal , chemical bond , polarization (electrochemistry) , chemical modification , peptide , crystallography , molecule , organic chemistry , enzyme , polymer chemistry , biochemistry , thermodynamics , physics , quantum mechanics , polymer
Abstract The possible influence of thermal motion on 1 H chemical shifts is discussed for a small stable protein, the bovine pancreatic Kunitz trypsin inhibitor (BPTI). The thermal effects on the aromatic side chains and on the backbone are treated separately. The thermal motion of the aromatic side chains is accounted for in terms of their rotation around the C α C β bond and the motion of each individual proton is interpreted as a ratio between the amount of ordered and quite disordered states. The influence of hydrogen bonds is introduced as an extra contribution to the chemical shifts of the bonded proton. Their contribution to the chemical shifts resulting from the polarization of the peptide bond is investigated, as is their influence on local flexibility. Finally, the relative importance of each contribution to the chemical shift information is compared. Copyright © 2001 European Peptide Society and John Wiley & Sons, Ltd.