title: Solution structure of the loops of bacteriorhodopsin closely resembles the crystal structure.
abstract: Bacteriorhodopsin is one of very few transmembrane proteins for which high resolution structures have been solved. The structure shows a bundle of seven helices connected by six turns. Some turns in proteins are stabilized by short range interactions and can behave as small domains. These observations suggest that peptides containing the sequence of the turns in a membrane protein such as bacteriorhodopsin may form stable turn structures in solution. To test this hypothesis, we determined the solution structure of three peptides each containing the sequence of one of the turns in bacteriorhodopsin. The solution structures of the peptides closely resemble the structures of the corresponding turns in the high resolution structures of the intact protein.
authors.affiliation: Department of Molecular and Cell Biology, University of Connecticut, Storrs 06269, USA.
authors.forename: M
authors.initials: M
authors.lastname: Katragadda
authors.forename: J L
authors.initials: JL
authors.lastname: Alderfer
authors.forename: P L
authors.initials: PL
authors.lastname: Yeagle
mesh_terms: D000595:Amino Acid Sequence; D001436:Bacteriorhodopsins / Q000737:chemistry*; D003460:Crystallization; D019617:Halobacterium salinarum / Q000737:chemistry*; D019077:Helix-Turn-Helix Motifs; D008958:Models, Molecular; D008969:Molecular Sequence Data; D019906:Nuclear Magnetic Resonance, Biomolecular / Q000379:methods; D010455:Peptides / Q000737:chemistry*; D017433:Protein Structure, Secondary; D012996:Solutions
chemical_list: D010455:Peptides; D012996:Solutions; D001436:Bacteriorhodopsins