Residual Dipolar Couplings for Resolving Cysteine Bridges in Disulfide-Rich Peptides.

ABSTRACT: Disulfide bridges in proteins are formed by the oxidation of pairs of cysteine residues. These cross-links play a critical role in stabilizing the 3D-structure of small disulfide rich polypeptides such as hormones and venom toxins. The arrangement of the multiple disulfide bonds directs the peptide fold into distinct structural motifs that have evolved for resistance against biochemical and physical insults. These structural scaffolds have, therefore, proven to be very attractive in bioengineering efforts to develop novel biologics with applications in health and agriculture. Structural characterization of small disulfide rich peptides (DRPs) presents unique challenges when using commonly applied biophysical methods. NMR is the most commonly used method for studying such molecules, where t

SUBMITTER: Ramanujam V 

PROVIDER: S-EPMC6987419 | biostudies-literature | 2019

REPOSITORIES: biostudies-literature