Solution structure of the loops of bacteriorhodopsin closely resembles the crystal structure

• Published in: Biochimica et biophysica acta Vol. 1466; no. 1; pp. 1 - 6
• Main Authors: Katragadda, Madan, Alderfer, James L., Yeagle, Philip L.
• Format: Journal Article
• Language: English
• Published: Netherlands Elsevier B.V 01.06.2000
• Subjects: Amino Acid Sequence; Bacteriorhodopsin; Bacteriorhodopsins - chemistry; Crystallization; Halobacterium salinarum - chemistry; Helix-Turn-Helix Motifs; Membrane protein; Models, Molecular; Molecular Sequence Data; NMR; Nuclear Magnetic Resonance, Biomolecular - methods; Peptides - chemistry; Protein Structure, Secondary; Solutions; Structure; Bacteriorhodopsin; NMR; Membrane protein; Structure
• ISSN: 0005-2736; 0006-3002; 1879-2642
• DOI: 10.1016/S0005-2736(00)00167-X

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.