Secondary structure of bacteriorhodopsin fragments: External sequence constraints specify the conformation of transmembrane helices

Journal of Biological Chemistry

Volumn 273, Issue 44, 1998, Pages 28822-28830

  Lüneberg, Jürgen ^a   Widmann, Margit ^b   Dathe, Margitta ^c   Marti, Thomas ^a  

^a BERNHARD NOCHT INSTITUTE FOR TROPICAL MEDICINE   (Germany)

^b UNIVERSITY OF ZURICH   (Switzerland)

^c LEIBNIZ INSTITUT FÜR MOLEKULARE PHARMAKOLOGIE   (Germany)

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIORHODOPSIN; MEMBRANE PROTEIN; PHOSPHOLIPID; POLYPEPTIDE;

ALPHA HELIX; AMINO ACID SEQUENCE; ARTICLE; CIRCULAR DICHROISM; CONTROLLED STUDY; FLUORESCENCE; MICELLE; PH; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN DOMAIN; PROTEIN FOLDING; PROTEIN SECONDARY STRUCTURE;

AMINO ACID SEQUENCE; BACTERIORHODOPSINS; CIRCULAR DICHROISM; HYDROGEN-ION CONCENTRATION; MOLECULAR SEQUENCE DATA; PEPTIDE FRAGMENTS; PROTEIN STRUCTURE, SECONDARY; SPECTROMETRY, FLUORESCENCE;

EID: 0032582541     PISSN: 00219258     EISSN: None     Source Type: Journal    
DOI: 10.1074/jbc.273.44.28822     Document Type: Article

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