Research Interest areas:
Protein crystallography
The crystal structure of the cytoplasmic cyclophilin-A, a peptidyl-prolyl isomerase, from Azotobacter vinelandii (AvCyPA) complexed with a synthetic tetrapeptide at 2.0 Å resolution. The diffraction pattern (1) from a bipyramidal shaped crystal of the protein indicates a tetragonal space group. The crystal structure of the AvCyPA/suc-AlaPheProPhe-pNA complex (PDB entry: 3T1U) (2) was solved by molecular replacement method and the protein-ligand interaction is visualized and analyzed with LigPlot (3).
(1) (2)
(3)
Inclusion chemistry
The physicochemical characterization (mainly by X-ray crystallography) of the inclusion compounds of agrochemicals, pharmaceutical and natural products in native and methylated cyclodextrins are under investigation. The crystal structure of the inclusion compound of the cholesterol molecule inside β-CD has been determined by X-ray crystallography (1) and structural studies of β-citronellol (essential oil from lemongrass) in native and methylated cyclodextrins have also been performed (2).
(1)
(2)