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A dihedral angle‐vicinal proton coupling constant correlation for the α–β bond of amino acid residues
Author(s) -
Kopple Kenneth D.,
Wiley Gary R.,
Tauke Ralph
Publication year - 1973
Publication title -
biopolymers
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.556
H-Index - 125
eISSN - 1097-0282
pISSN - 0006-3525
DOI - 10.1002/bip.1973.360120314
Subject(s) - dihedral angle , chemistry , vicinal , coupling constant , proton , limiting , crystallography , amino acid , peptide , amino acid residue , coupling (piping) , range (aeronautics) , stereochemistry , hydrogen bond , organic chemistry , molecule , peptide sequence , biochemistry , physics , mechanical engineering , particle physics , quantum mechanics , engineering , gene , materials science , composite material
A coupling constant‐dihedral angle correlation for the HCαCβH system of amino acid residues in peptides has been derived from a set of model compounds covering the full range of dihedral angles. The expression obtained, J = 11.0 cos 2 θ −1.4 cos θ + 1.6 sin 2 θ, is close to those already used in pmr studies of peptide conformation, and provides a firmer foundation for them. A factor limiting the precision of this and other “Karplus relations” is illustrated.