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Protein-ligand interaction investigated by HSQC titration study

Authors
Lee, Joon-Hwa
Issue Date
Dec-2018
Publisher
KOREAN MAGNETIC RESONANCE SOC
Keywords
NMR; chemical shift perturbation; protein-ligand interaction; HSQC; titration
Citation
JOURNAL OF THE KOREAN MAGNETIC RESONANCE SOCIETY, v.22, no.4, pp 125 - 131
Pages
7
Indexed
ESCI
KCI
Journal Title
JOURNAL OF THE KOREAN MAGNETIC RESONANCE SOCIETY
Volume
22
Number
4
Start Page
125
End Page
131
URI
https://scholarworks.gnu.ac.kr/handle/sw.gnu/11029
DOI
10.6564/JKMRS.2018.22.4.125
ISSN
1226-6531
Abstract
Chemical shift perturbation (CSP) is a simple NMR technique for studying binding of a protein to various ligands. CSP is the only technique that can directly provide both a value for the dissociation constant and a binding site from the same set of measurements. To accurately analyze the CSP data, the exact binding mode such as multiple binding, should be carefully considered. In this review, we analyzed systematically the CSP data with multiple modes. This analysis might provide insight into the mechanism on how proteins selectively recognize their target ligands to achieve the biological function.
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