A dihedral angle‐vicinal proton coupling constant correlation for the α–β bond of amino acid residues | Zendy

Kopple Kenneth D. | Zendy; Wiley Gary R. | Zendy; Tauke Ralph | Zendy

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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.

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