NMR Chemical Shift Mapping of SH2 Peptide Interactions.
Related Articles NMR Chemical Shift Mapping of SH2 Peptide Interactions.
Methods Mol Biol. 2017;1555:269-290
Authors: McKercher MA, Wuttke DS
Abstract
Heteronuclear single quantum coherence (HSQC) nuclear magnetic resonance (NMR) experiments offer a rapid and high resolution approach to gaining binding and conformational insights into a protein-peptide interaction. By tracking (1)H and (15)N chemical shift changes over the course of a peptide titration into isotopically labeled protein, amide NH pairs of amino acids whose chemical environment changes upon peptide binding can be identified. When mapped onto a structure of the protein, this approach can identify the peptide-binding interface or regions undergoing conformation changes within a protein upon ligand binding. Monitoring NMR chemical shift changes can also serve as a screening technique to identify novel interaction partners for a protein or to determine the binding affinity of a weak protein-peptide interaction. Here, we describe the application of NMR chemical shift mapping to the study of peptide binding to the C-terminal SH2 domain of PLC?1.
PMID: 28092038 [PubMed - in process]
More...