In situ investigation of transmembrane polypeptides using sum frequency generation spectroscopy

ANYL 127

Neil A. Anderson, neil.anderson@nist.gov1, Kimberly A. Briggman, kbriggma@nist.gov2, John C. Stephenson2, and Lee J. Richter, lee.richter@nist.gov3. (1) NIST, 100 Bureau Drive, MS8443, Gaithersburg, MD 20899, (2) Optical Technology Division, National Institute of Science and Technology, 100 Bureau Drive Stop 8443, Gaithersburg, MD 20899, (3) Surface and Microanalysis Science Division, National Institute of Standards and Technology, 100 Bureau Drive, Gaithersburg, MD 20899
Membrane proteins are extremely important in cell biology, but comparatively little is understood regarding their structures in native membrane environments. Vibrationally-resonant sum frequency generation spectroscopy (SFG) provides interfacial selectivity and chemical sensitivity and is being developed to allow tagless in situ investigation of membrane protein structures in supported bilayer membranes. In this work, engineered transmembrane polypeptides are inserted into hybrid bilayer membranes. SFG spectroscopy is used to monitor the kinetics of polypeptide incorporation into membranes of varying fluidities. Furthermore, the spectra allow determination of polypeptide secondary structure and orientation within the membrane.
 

General Papers
7:00 PM-9:00 PM, Sunday, 28 August 2005 Washington DC Convention Center -- Hall A, Poster

Division of Analytical Chemistry

The 230th ACS National Meeting, in Washington, DC, Aug 28-Sept 1, 2005