Uniformly aligned full-length membrane proteins in liquid crystalline bilayers for structural characterization

Conggang Li; Philip Gao; Huajun Qin; Rose Chase; Peter L Gor'kov; William W Brey; Timothy A Cross

doi:10.1021/ja068402f

Uniformly aligned full-length membrane proteins in liquid crystalline bilayers for structural characterization

J Am Chem Soc. 2007 May 2;129(17):5304-5. doi: 10.1021/ja068402f. Epub 2007 Apr 4.

Authors

Conggang Li¹, Philip Gao, Huajun Qin, Rose Chase, Peter L Gor'kov, William W Brey, Timothy A Cross

Affiliation

¹ Department of Chemistry and Biochemistry and Institute of Molecular Biophysics, Florida State University, Tallahassee, Florida 32306, USA.

Abstract

High-resolution solid-state NMR spectra of three full-length membrane proteins uniformly aligned in lipid bilayers between glass slides are observed at high magnetic field. The resolution of the specific amino acid labeled samples shows promise for large membrane protein structure determination utilizing aligned samples and shows resonance patterns known as PISA wheels. The tilt angles of the transmembrane helices are extracted from the resonance patterns in PISEMA spectra.

Publication types

Research Support, N.I.H., Extramural
Research Support, Non-U.S. Gov't
Research Support, U.S. Gov't, Non-P.H.S.

MeSH terms

Amino Acid Sequence
Diacylglycerol Kinase / chemistry
Escherichia coli / chemistry
Escherichia coli / genetics
Liquid Crystals / chemistry*
Magnetic Resonance Spectroscopy
Membrane Proteins / chemistry*
Membranes, Artificial
Molecular Sequence Data
Molecular Weight
Mycobacterium tuberculosis / chemistry
Mycobacterium tuberculosis / genetics
Protein Conformation

Substances

Membrane Proteins
Membranes, Artificial
Diacylglycerol Kinase

Abstract

Publication types

MeSH terms

Substances

Grants and funding