NMR characterization of the electrostatic interaction of the basic residues in HDGF and FGF2 during heparin binding.

@article{Chiu2014NMRCO,
  title={NMR characterization of the electrostatic interaction of the basic residues in HDGF and FGF2 during heparin binding.},
  author={Liang-Yuan Chiu and Kuo-Wei Hung and Siu-Cin Tjong and Yun-Wei Chiang and Shih-Che Sue},
  journal={Biochimica et biophysica acta},
  year={2014},
  volume={1844 10},
  pages={
          1851-9
        }
}
Electrostatic interaction is a major driving force in the binding of proteins to highly acidic glycosaminoglycan, such as heparin. Although NMR backbone chemical shifts have generally been used to identify the heparin-binding site on a protein, however, there is no correlation between the binding free energies and the perturbed backbone chemical shifts for individual residues. The binding event occurs at the end of a side chain of basic residue, and does not require causing significant… CONTINUE READING

References

Publications referenced by this paper.
Showing 1-10 of 37 references

Bonvin, HADDOCK versus HADDOCK: new features and performance of HADDOCK2.0 on the CAPRI targets, Proteins

S. J. de Vries, A. D. van Dijk, +4 authors A.M.T. Wassenaar
2007
View 6 Excerpts
Highly Influenced

Using chemical shift perturbation to characterise ligand binding.

Progress in nuclear magnetic resonance spectroscopy • 2013
View 2 Excerpts

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