Journal of the Korean Magnetic Resonance Society (한국자기공명학회논문지)

Korean Magnetic Resonance Society (한국자기공명학회)
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Molecular Dynamics of the C-Terminal Domain Mouse CDT1 Protein

  • Khayrutdinov, Bulat I. (The Magnetic Resonance Team, Korea Basic Science Institute) ;
  • Bae, Won-Jin (National Creative Research Center for Structural Biology and Department of Life Science, Pohang University of Science and Technology) ;
  • Kim, Jeong-Ju (National Creative Research Center for Structural Biology and Department of Life Science, Pohang University of Science and Technology) ;
  • Hwang, Eun-Ha (The Magnetic Resonance Team, Korea Basic Science Institute) ;
  • Yun, Young-Mi (National Creative Research Center for Structural Biology and Department of Life Science, Pohang University of Science and Technology) ;
  • Ryu, Kyoung-Seok (The Magnetic Resonance Team, Korea Basic Science Institute) ;
  • Cheong, Hae-Kap (The Magnetic Resonance Team, Korea Basic Science Institute) ;
  • Kim, Yu-Gene (National Creative Research Center for Structural Biology and Department of Life Science, Pohang University of Science and Technology) ;
  • Cho, Yun-Je (National Creative Research Center for Structural Biology and Department of Life Science, Pohang University of Science and Technology) ;
  • Jeon, Young-Ho (The Magnetic Resonance Team, Korea Basic Science Institute) ;
  • Cheong, Chae-Joon (The Magnetic Resonance Team, Korea Basic Science Institute)
  • Published : 2007.06.20
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Abstract

The backbone molecular dynamics of the C-terminal part of the mouse Cdt1 protein (tCdt1, residues 420-557) was studied by high field NMR spectroscopy. The Secondary structure of this protein was suggested by analyzing of chemical shift of backbone atoms with programs TALOS and PECAN, together with NOE connectivities from 3D $^{15}N-HSQC-NOESY$ data. Measurement of dynamic parameters $T_1,\;T_2$ and NOE and limited proteolysis experiment provided information for domain organization of tCdt1(420-557). Analysis of the experimental data showed that the C-terminal part of the tCdt1 has well folded domain for residues 455-553. The residues 420-453 including ${\alpha}-helix$ (432-441) are flexible and probably belong to other functional domain in intact full length Cdt1 protein.

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