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Protein-ligand interaction investigated by HSQC titration study

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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.

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.

참고문헌 (6)

  1. M. P. Williamson, , Prog. Nuclear Magn. Reson. Spec., 73, pp.1~ (2013)
  2. E. R. P. Zuiderweg, , Biochemistry, 41, pp.1~ (2002)
  3. M. A. McCoy, , J. Am. Chem. Soc., 124, pp.11758~ (2002)
  4. M. Arai, , J. Am. Chem. Soc., 134, pp.3792~ (2012)
  5. J. Granot, , J. Magn. Reson., 55, pp.216~ (1983)
  6. L. Fielding, , Prog. Nucl. Magn. Reson. Spectrosc, 51, pp.219~ (2007)

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