Chapter title |
NMR Chemical Shift Mapping of SH2 Peptide Interactions
|
---|---|
Chapter number | 15 |
Book title |
SH2 Domains
|
Published in |
Methods in molecular biology, January 2017
|
DOI | 10.1007/978-1-4939-6762-9_15 |
Pubmed ID | |
Book ISBNs |
978-1-4939-6760-5, 978-1-4939-6762-9
|
Authors |
Marissa A. McKercher, Deborah S. Wuttke |
Editors |
Kazuya Machida, Bernard A. Liu |
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 PLCγ1. |
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