Journal of the Korean Magnetic Resonance Society (한국자기공명학회논문지)

Korean Magnetic Resonance Society (한국자기공명학회)
권호 표지
DOI QR코드

DOI QR Code

Elucidating the Dynamic Properties of Globular Protein using Predicted Order Parameters and 15N NMR Relaxation

  • Yi, Jong-Jae (College of pharmacy, CHA University) ;
  • Kim, Won-Je (College of pharmacy, Seoul National University) ;
  • Rhee, Jin-Kyu (Department of Food Science and Engineering, Ewha Womans University) ;
  • Lim, Jongsoo (Discovery Technology Team, Dong-A ST Research Institute) ;
  • Lee, Bong-Jin (College of pharmacy, Seoul National University) ;
  • Son, Woo Sung (College of pharmacy, CHA University)
  • Received : 2017.02.12
  • Accepted : 2017.03.12
  • Published : 2017.03.20
Download PDF
⟨ Previous Next ⟩

Abstract

Dynamic properties of proteins can present key information on protein-ligand and protein-protein interaction. Despite their usefulness, the properties of protein dynamics have not been obtained easily due to protein stability and short-term measurement. Here, it is shown that combined method for analysis of dynamical properties. It utilizes predicted order parameter and NMR relaxation data such as $T_1$, $T_2$, and heteronuclear NOE. The suggested method could be used to know the flexibility of protein roughly without precise dynamical parameters such as order parameters through model-free analysis.

Keywords

References

  1. Z. Bu, and D. J. Callaway, Adv. Protein Chem. Str. 83, 163 (2011)
  2. J. S. Fraser, M. M. Clarkson M. W, S. C. Degnan, R. Erion, D. Kern, and T. Alber, Nature 462, 669 (2009) https://doi.org/10.1038/nature08615
  3. J. G. Torre, P. Bernado, and M. Pons, Methods Enzymol. 394, 419 (2005)
  4. G. Lipari, and A. Szabo, J. Am. Chem. Soc. 104, 4546 (1982) https://doi.org/10.1021/ja00381a009
  5. A. G. Palmer, J. Williams, and A. McDermott, J. Am. Chem. Soc. 100, 13293 (1996)
  6. F. Zhang, and R. Bruschweiler, J. Am. Chem. Soc. 124, 12654 (2002) https://doi.org/10.1021/ja027847a
  7. J. Yi, J. K. Yoo, J. K. Kim, and W. S. Son, J. Kor. Magn. Reson. Soc. 17, 30 (2013) https://doi.org/10.6564/JKMRS.2013.17.1.030
  8. W. Kim, J. Rhee, J. Yi, B. Lee, and W. S. Son, J. Kor. Magn. Reson. Soc. 18, 36 (2014) https://doi.org/10.6564/JKMRS.2014.18.1.036
  9. P. Dosset, J. Hus, M. Blackledge, and D. Marion, J. Biomol. NMR 16, 23 (2000) https://doi.org/10.1023/A:1008305808620
  10. F. Cordier, M. Caffrey, B. Brutscher, M. A. Cusanovich, D. Marion, and M. Blackledge, J. Mol. Biol. 281, 341 (1998) https://doi.org/10.1006/jmbi.1998.1950
  11. P. Tsan, J. Hus, M. Caffrey, D. Marion, and M. Blackledge, J. Am. Chem. Soc. 122, 5603 (2000) https://doi.org/10.1021/ja993654k
  12. M. Blackledge, F. Cordier, P. Dosset, and D. Marion, J. Am. Chem. Soc. 120, 4538 (1998) https://doi.org/10.1021/ja9742646
  13. J. L. Goodman, M. D. Pagel, and M. J. Stone, J. Mol. Biol. 295, 963 (2000) https://doi.org/10.1006/jmbi.1999.3419
  14. A. Sali, and T. L. Blundell, J. Mol. Biol. 234, 779 (1993) https://doi.org/10.1006/jmbi.1993.1626