Major Interests:
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. |
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Publications:
Rhee JE, Sheng W, Morgan LK, Nolet R, Liao X, Kenney LJ. (2008)Amino acids
important for DNA recognition by the response regulator OmpR. J Biol Chem.
2008 Mar 28;283(13):8664-77.
Carroll RK, Liao X, Morgan LK, Cicirelli E, Li Y, Sheng W, Feng X, Kenney
LJ. (2009) Structural and functional analysis of the C-terminal DNA
binding domain of the salmonella typhimurium SPI-2 response regulator
SsrB. J Biol Chem. 284(18):12008-19
Jin T, Ito Y, Luan X, Dangaria S, Walker C, Allen M, Kulkarni A, Gibson
C, Braatz R, Liao X, and Diekwisch TGH (2009 ) Elongated Polyproline
Motifs Facilitate Enamel Evolution through Matrix Subunit Compaction
PLoS Biol. 7(12):e1000262.
Zhang X, Ramirez B, Liao X, and Diekwisch TGH (2011) Amelogenin
Supramolecular Assembly in Nanospheres 1 Defined by a Complex
Helix-Coil-PPII helix 3D-Structure PLoS Biol. 2011;6(10):e24952
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