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Pei Zhou

Associate Professor
Research Interest: 
Molecular structure
Research Summary: 
NMR methodology and its application to understanding the molecular recognition of essential protein complexes in crucial biological processes.
Research Description: 

Protein-protein interactions play a pivotal role in the regulation of cellular processes. The formation of higher-order protein complexes is frequently accompanied by extensive structural remodeling of individual components, varying from domain re-orientation to binding-induced folding of unstructured elements. NMR spectroscopy not only is a powerful tool for macromolecular structure determination in solution, but also provides valuable information on conformational dynamics associated with the process of molecular recognition. Recent advances in NMR techniques have led to faster and more accurate structure determination and have greatly facilitated the studies of protein complexes in crucial biomedical processes.

Lipooligosaccharide is required for the generation of infectious elementary bodies in Chlamydia trachomatis.
Nguyen BD, Cunningham D, Liang X, Chen X, Toone EJ, Raetz CR, Zhou P, Valdivia RH.
Proc Natl Acad Sci U S A. 2011. 108:10284-9.

Species-specific and inhibitor-dependent conformations of LpxC: implications for antibiotic design.
Lee CJ, Liang X, Chen X, Zeng D, Joo SH, Chung HS, Barb AW, Swanson SM, Nicholas RA, Li Y, Toone EJ, Raetz CR, Zhou P.
Chem Biol. 2011. 18:38-47.

cis-Proline-mediated Ser(P)5 dephosphorylation by the RNA polymerase II C-terminal domain phosphatase Ssu72.
Werner-Allen JW, Lee CJ, Liu P, Nicely NI, Wang S, Greenleaf AL, Zhou P.
J Biol Chem. 2011. 286:5717-26.

Unconventional ubiquitin recognition by the ubiquitin-binding motif within the Y family DNA polymerases iota and Rev1.
Bomar MG, D'Souza S, Bienko M, Dikic I, Walker GC, Zhou P.
Mol Cell. 2010. 37:408-17.

Radial sampling for fast NMR: Concepts and practices over three decades.
Coggins BE, Venters RA, Zhou P.
Prog Nucl Magn Reson Spectrosc. 2010. 57:381-419.