Contact Information

University Of Illinois at Chicago

Dept. Of Biochemistry and

Molecular Genetics

900 S. Ashland (M/C 669)
Chicago, IL 60607
tel: 312-996-7670
fax: 312-413-0353

Biochemical and NMR studies of protein structure and function, protein-nucleic acid and protein-protein interactions.

Research in the field of macromolecule structure has progressed very rapidly. X-ray diffraction techniques have been successfully used to study the crystal structure of number of macromolecules, but methods to determine solution structures of macromolecules had previously been limited. Recent technical improvements in high resolution NMR spectroscopy combined with molecular biology techniques provide powerful tools to study the structure and dynamics of macromolecules. Since NMR is very sensitive to local conformational changes and gives direct information on the tertiary structure and dynamics of macromolecules in solution, it plays an increasingly important role in these studies. A focus of this laboratory involves studies of protein-nucleic acid interactions by a combination of NMR and biochemical techniques. NMR is used to study the structure and dynamics of both the free protein and the protein-nucleic acid complex. The biochemical techniques are used to relate the structure to its function.

Selected Publications:

Bravieri B, Shiyanova T, Chen TH, Overdier D, and Liao X (1997): Different DNA contact schemes are used by two winged helix proteins to recognize a DNA binding sequence. Nucl Acids Res. 25:2888Ð2896.

Marsden I, Chen Y, Jin C, and Liao X (1997): Evidence that the DNA binding specificity of winged helix proteins is mediated by a structural change in the amino acid sequence adjacent to the principal DNA binding helix. Biochemistry. 36:13248Ð13255.

Marsden I, Jin C, and Liao X (1998): Structural changes in the region directly adjacent to the DNA binding helix highlight a possible mechanism to explain the observed changes in the sequence-specific binding of winged helix proteins. J Mol Biol. 278, 293Ð299.

Jin C, Marsden I, Chen X, and Liao X (1998): Sequence specific collective motions in a winged helix DNA binding domain detected by 15N relaxation NMR. Biochemistry. 37:6179Ð6187.

Shiyanova T and Liao X (1999): The dissociation rate of a winged helix protein-DNA complex is influenced by non-DNA contact residues. Arch Biochem Biophysics. 362:356Ð362.

Jin C, Marsden I, Chen X, and Liao X (1999): Dynamic DNA contacts observed in the NMR structure of a winged helix protein-DNA complex. J Mol Biol. 289:683Ð690.