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

✍ Scribed by Kenneth D. Kopple; Gary R. Wiley; Ralph Tauke

Publisher
Wiley (John Wiley & Sons)
Year
1973
Tongue
English
Weight
512 KB
Volume
12
Category
Article
ISSN
0006-3525

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✦ Synopsis

Abstract

A coupling constant‐dihedral angle correlation for the HCαCβH 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.

📜 SIMILAR VOLUMES

Conformational dependence of the vicinal
Conformational dependence of the vicinal proton coupling constant for the CαCβ bond in peptides
✍ M. T. Cung; M. Marraud 📂 Article 📅 1982 🏛 Wiley (John Wiley & Sons) 🌐 English ⚖ 680 KB

## Abstract We use the nmr data concerning the C^α^HC^β^H fragment in eight peptides with rigid side chains to parametrize a Karplus correlation between the vicinal proton __J__~αβ~ coupling constant and the dihedral angle θ. When considering molecules containing the fragment C^α^H^α^C^β^H^β^H^β′

Dihedral-angle dependence of the vicinal
Dihedral-angle dependence of the vicinal 15N,13C spin-coupling constants. A new NMR parameter for the conformational analysis of amino acids and peptides
✍ Masatsune Kainosho; Takashi Tsuji 📂 Article 📅 1981 🏛 John Wiley and Sons 🌐 English ⚖ 394 KB

## Abstract The first successful observation of the vicinal ^15^N,^13^C spin‐coupling constants in a series of amino acids, comprising Val, Ile, Leu and Thr, in which the α‐nitrogens are fully replaced with ^15^N, is described. A Karplus‐type dihedral‐angle dependence was noted for the coupling con