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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