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  English.dicp.cas.cn    Posted:2016-07-14
Using single molecule FRET study the conformational dynamics of FimD

Time:3:00 pm, July. 14th of 2016

Location:Conference room in Biotechnology Building

Prof. Yongfang Zhao,

National laboratory of biomacromolecules,

Institute of Biophysics, Chinese Academy of Science

Abstract:

The chaperone/usher pathway is a conserved bacterial secretion system that assembles adhesive fibers termed pili or fimbriae. The usher catalyzes formation of subunit-subunit interactions to promote polymerization of the pilus fiber and provides the channel for the fiber secretion. The mechanism by which the usher catalyzes pilus assembly is not known. Using single molecule FRET method, we studied the conformational dynamics of usher FimD before and after formation of complexes. Our results suggested that the N terminal domain and C terminal domain together regulate the position of the plug domain.

Introduction:

EDUCATION

1999-2004 Ph. D. in Biochemistry and Molecular Biology, State Key Laboratory of Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences;

1995-1999 Bachelor of Biochemistry and Biophysics, School of Life Science, Wuhan University

WORKING EXPERENCE

2013-present Professor, Institute of Biophysics, CAS

2009-2013 Associate Research Scientist, Department of Psychiatry, Center for Molecular Recognition, Columbia University

2005-2009 Postdoctoral Research Fellow, Center for Molecular Recognition, Columbia University

RESEARCH INTEREST:

The main research focus of our group is on structural and functional studies of 1) membrane protein using single molecular FRET (smFRET); 2) GPCR (especially chemokine receptors) dimerization on cell level.

AWARDS

Contact: 1818 Yin Wenting (9648)

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