Structural Studies on Large Fragments of G Protein Coupled Receptors
The use of peptide fragments to study the biophysical and structural properties of regions of polytopic membrane proteins is widespread [1,2]. In most cases these studies have been limited to synthetic peptides containing 20–40 amino acid residues. Moreover, although some high resolution structures of fragments corresponding to single transmembrane regions of membrane proteins in organic-aqueous membrane mimetic solvents have appeared, there are few such structures from studies in detergent micelles. Although important information is obtained from studies on membrane peptides in media such as trifluoroethanol-water and dimethylsulfoxide, it is highly desirable to compare such structures to those obtained in micelles and bicelles. Furthermore, since long range interhelical interactions can influence the structures of individual transmembrane domains, investigations on peptides containing multiple transmembrane regions of integral membrane proteins are necessary.
KeywordsHSQC Spectrum Intracellular Loop Putative Transmembrane Domain Chemical Shift Indexing Polytopic Membrane Protein
This work was supported by grants NIH GM-22086 and NIH GM-22087 to FN and JMB.
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