Quantifying residue-specific conformational dynamics of a highly reactive 29-mer peptide.

ABSTRACT: Understanding structural transitions within macromolecules remains an important challenge in biochemistry, with important implications for drug development and medicine. Insight into molecular behavior often requires residue-specific dynamics measurement at micromolar concentrations. We studied MP01-Gen4, a library peptide selected to rapidly undergo bioconjugation, by using electron paramagnetic resonance (EPR) to measure conformational dynamics. We mapped the dynamics of MP01-Gen4 with residue-specificity and identified the regions involved in a structural transformation related to the conjugation reaction. Upon reaction, the conformational dynamics of residues near the termini slow significantly more than central residues, indicating that the reaction induces a structural transition far

SUBMITTER: Lindemann WR 

PROVIDER: S-EPMC7018720 | biostudies-literature | 2020 Feb

REPOSITORIES: biostudies-literature