Conformational Analysis of Uniformly ¹³C-Labeled Peptides by Rotationally Selected ¹³Cα-¹³CH₃ Double-Quantum Solid-State NMR.

ABSTRACT: Peptides are an important class of biomolecules that perform many physiological functions and which occupy a significant and increasing share of the pharmaceutical market. Methods to determine the solid-state structures of peptides in different environments are important to help understand their biological functions and to aid the development of drug formulations. Here, a new magic-angle spinning (MAS) solid-state nuclear magnetic resonance (SSNMR) approach is described for the structural analysis of uniformly ¹³C-labeled solid peptides. Double-quantum (DQ) coherence between selective pairs of ¹³C nuclei in peptide backbone and side-chain CH₃ groups is excited to provide restraints on (i) ¹³C-¹³C internuclear distances and (ii) the rel

SUBMITTER: Middleton D 

PROVIDER: S-EPMC11820148 | biostudies-literature | 2025 Feb

REPOSITORIES: biostudies-literature