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Conformation of surface exposed N‐terminus part of bacteriorhodopsin studied by transferred NOE technique
Author(s) -
Pashkov Vladimir S.,
Balashova Tamara A.,
Zhemaeva Ljubov V.,
Sikilinda Ni.,
Kutuzov Michail A.,
Abdulaev Najmoutin G.,
Arseniev Alexander S.
Publication year - 1996
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(96)00094-4
Subject(s) - bacteriorhodopsin , chemistry , peptide , nuclear overhauser effect , pulse sequence , transmembrane protein , peptide sequence , sequence (biology) , n terminus , stereochemistry , crystallography , nuclear magnetic resonance spectroscopy , nuclear magnetic resonance , biochemistry , membrane , physics , gene , receptor
Interaction of the monoclonal antibody A5 raised against native bacteriorhodopsin (BR) with the synthetic peptide pGlu 1 ‐Ala‐Gln‐Ile‐Thr‐Gly‐Arg 7 ‐NH 2 , corresponding to the amino acid sequence 1–7 was studied by transferred nuclear Overhauser effect (TRNOE) spectroscopy. The denaturing reagents and the specially designed pulse sequences which eliminate broad signals from the TRNOE spectra were used to favour evaluation of the TRNOE peaks. On the basis of the data obtained, the conformation of peptide bound with A5 was calculated. A model of the mutual arrangement of bacteriorhodopsin N‐terminus and the first transmembrane α‐helical segment 8–32 was proposed.