Toward a Computational NMR Procedure for Modeling Dipeptide Side-Chain Conformation.

ABSTRACT: Theoretical relationships between the vicinal spin-spin coupling constants (SSCCs) and the χ₁ torsion angles have been studied to predict the conformations of protein side chains. An efficient computational procedure is developed to obtain the conformation of dipeptides through theoretical and experimental SSCCs, Karplus equations, and quantum chemistry methods, and it is applied to three aliphatic hydrophobic residues (Val, Leu, and Ile). Three models are proposed: unimodal-static, trimodal-static-stepped, and trimodal-static-trigonal, where the most important factors are incorporated (coupled nuclei, nature and orientation of the substituents, and local geometric properties). Our results are validated by comparison with NMR and X-ray empirical data described in the literature,

SUBMITTER: San Fabian J 

PROVIDER: S-EPMC8715507 | biostudies-literature | 2021 Dec

REPOSITORIES: biostudies-literature