Solution structure of the loops of bacteriorhodopsin closely resembles thecrystal structure

Citation
M. Katragadda et al., Solution structure of the loops of bacteriorhodopsin closely resembles thecrystal structure, BBA-BIOMEMB, 1466(1-2), 2000, pp. 1-6
Citations number
12
Categorie Soggetti
Biochemistry & Biophysics
Journal title
BIOCHIMICA ET BIOPHYSICA ACTA-BIOMEMBRANES
ISSN journal
00052736 → ACNP
Volume
1466
Issue
1-2
Year of publication
2000
Pages
1 - 6
Database
ISI
SICI code
0005-2736(20000601)1466:1-2<1:SSOTLO>2.0.ZU;2-L
Abstract
Bacteriorhodopsin is one of very few transmembrane proteins for which high resolution structures have been solved. The structure shows a bundle of sev en helices connected by six turns. Some turns in proteins are stabilized by short range interactions and can behave as small domains. These observatio ns suggest that peptides containing the sequence of the turns in a membrane protein such as bacteriorhodopsin may form stable turn structures in solut ion. To test this hypothesis, we determined the solution structure of three peptides each containing the sequence of one of the turns in bacteriorhodo psin. The solution structures of the peptides closely resemble the structur es of the corresponding turns in the high resolution structures of the inta ct protein. (C) 2000 Elsevier Science B.V. All rights reserved.