Modeling pH-Dependent NMR Chemical Shift Perturbations in Peptides.

ABSTRACT: Modeling the pH dependence of protein and peptide chemical shifts outside the range of physiological values (6.5-7) is key to understanding structure-function relationships of these systems. These capabilities are largely not available in current chemical shift prediction software. In this study, we utilize a combination of molecular dynamics and quantum mechanics to investigate the through-space and through-bond contributions of protonation-dependent chemical shift perturbations (CSPs) in model tripeptides. By altering the protonation state of the titratable group in the tripeptides, we observe a notable difference in the conformational ensembles and attendantly compute significant CSPs for all nuclei near the site of protonation. We thus demonstrate the ability to recapitulate experiment

SUBMITTER: Artikis E 

PROVIDER: S-EPMC6700603 | biostudies-literature | 2019 Jul

REPOSITORIES: biostudies-literature