Component Vicinal Coupling Constants for Calculating Side-chain Conformations in Amino Acids

Overview

Journal Int J Pept Protein Res

Date 1982 Aug 1

PMID 7118434

Citations 3

Authors

F A de Leeuw

C Altona

Affiliations

Soon will be listed here.

Abstract

The averaged proton-proton torsion angles for the three side-chain rotamers in amino acids are calculated from a statistical analysis of X-ray structures of side-chain fragments. In combination with a generalized Karplus equation the limiting coupling constants for the rotamers are calculated. The presently deduced sets are compared with published sets of limiting coupling constants.

Citing Articles

Synthesis and Reactivity of α-Haloglycine Esters: Hyperconjugation in Action.

Samanta S, Roche S European J Org Chem. 2020; 2019(39):6597-6605.

PMID: 32351314 PMC: 7189931. DOI: 10.1002/ejoc.201901033.

Structure-activity relationships of bifunctional cyclic disulfide peptides based on overlapping pharmacophores at opioid and cholecystokinin receptors.

Agnes R, Ying J, Kover K, Lee Y, Davis P, Ma S Peptides. 2008; 29(8):1413-23.

PMID: 18502541 PMC: 2601673. DOI: 10.1016/j.peptides.2008.03.022.

Side-chain conformational thermodynamics of aspartic acid residue in the peptides and achatin-I in aqueous solution.

Kimura T, Matubayasi N, Nakahara M Biophys J. 2004; 86(2):1124-37.

PMID: 14747347 PMC: 1303905. DOI: 10.1016/S0006-3495(04)74187-9.