2001-2002
2002-2003
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Seth Robia, Ph.D.
Intrasequence GFP in class I MHC molecules, a rigid
probe for fluorescence anisotropy measurements of the
membrane environment.
Rocheleau, J. V., M. Edidin, and D. W. Piston.
Biophysical Journal 84:4078-4086 (2003).
A recent paper by Rocheleau et al. describes the use
of an intrasequence green fluorescent protein (GFP)
rigidly fused to major histocompatibility complex (MHC)
class I molecules as an anisotropic tag for measuring
clustering of MHC. Assembly of tagged MHC-I molecules
results in Fluorescence Resonance Energy Transfer (FRET)
between proximate GFPs, detected as a decreased
anisotropy of the fluorescence emission. This study
demonstrates the utility of polarized fluorescence
imaging as a tool for in vivo structural biology. I will
discuss this paper in the context of some of our recent
experiments in the Thomas lab, in which we investigate
the quaternary conformation of phospholamban pentamers
by in-gel anisotropy.
Date: December 15th
Time: Noon to 1
Place: BSBE 4-101
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