Laboratories & Administration Office

Laboratory of Structural Proteomics

member

Associate Professor Takahisa IKEGAMI
Instructor Naotoshi MIMURA
Akiko OKUMURA
Young-Ho LEE

Correspondence

Tel 81-6-6879-8598
Fax 81-6-6879-8600
E-mail
URL http://www.protein.osaka-u.ac.jp/rcsfp/structure/nmr/english/english.html

Research

We mainly determine the three-dimensional structures of proteins and peptides using nuclear magnetic resonance spectroscopy (NMR). In addition, we are studying the interaction of a protein with another protein or its substrate. NMR is also suitable for analyses of flexibility, providing information as to which parts of proteins fluctuate. We are especially interested in slow dynamics, which can be directly related to the protein activities. Furthermore, the developments of NMR methodologies to facilitate the above studies are also important tasks.


<Fig.1>
The 800MHz NMR machine containing a superconducting magnet and
cryogenic probe. Its sensitivity amounts to about 10-times that exhibited by a
normal 400MHz machine. The machine is therefore used for diluted samples
within a shorter period, and for isotopically non-labeled samples.


<Fig.2>
Estimation of the dihedral angles of the main-chain from the cross-correlated
relaxation rates between CαHα and NH. The ratio of the peak intensity for the
cross-correlated spectrum (right) to that for the reference spectrum (left) is a
function of the associated dihedral angle ψ.

Current Research Programs

1) Analyses of structures and dynamics of proteins
2) Analyses of the interactions between proteins and other related molecules
3) Development of related NMR methodology
4) Structural analysis of nNOS in the complex form with an associated protein

References

1. Structure of the cadherin-related neuronal receptor/ protocadherin-alpha first extracellular cadherin domain reveals diversity across cadherin families. Morishita, H. et al. (2006) J. Biol. Chem. 281, 33650-33663.
2. Orexin-A is composed of a highly conserved C-terminal and a specific, hydrophilic N-terminal region, revealing the structural basis of specific recognition by the orexin-1 receptor. Takai, T. et al. (2006) J. Pept. Sci. 12, 443-454.
3. Identification of the substrate interaction region of the chitin-binding domain of Streptomyces griseus chitinase C. Akagi, K. et al. (2006) J. Biochem. 139, 483-493.

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