Orientation and Motion of Tryptophan Interfacial Anchors in Membrane-Spanning Peptides †
✍ Scribed by van der Wel, Patrick C. A.; Reed, Nicole D.; Greathouse, Denise V.; Koeppe, Roger E.
- Book ID
- 126437732
- Publisher
- American Chemical Society
- Year
- 2007
- Tongue
- English
- Weight
- 313 KB
- Volume
- 46
- Category
- Article
- ISSN
- 0006-2960
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## Abstract Solid‐state NMR spectroscopy is used to determine the structures of membrane peptides and proteins in lipid bilayers. The methodology for membrane protein structure determination using solid‐state NMR of oriented lipid bilayer samples is outlined. Recent developments in recombinant bact
Fluorescence quenching is used to gain information on the exposure of tryptophan residues to lipid in membrane-bound proteins and peptides. A protocol is developed to calculate this exposure, based on a comparison of quenching efficiency and of a fluorescence lifetime (or quantum yield) measured for