Conformation of surface exposed N-terminus part of bacteriorhodopsin studied by transferred NOE technique
| Autor: | T. A. Balashova, Alexander S. Arseniev, Nina N. Sikilinda, Ljubov V. Zhemaeva, Michail A. Kutuzov, N.G. Abdulaev, Vladimir S. Pashkov |
|---|---|
| Jazyk: | angličtina |
| Předmět: |
Models
Molecular Monoclonal antibody Magnetic Resonance Spectroscopy Stereochemistry Spatial structure Molecular Sequence Data Biophysics Bacteriorhodopsin Peptide Nuclear Overhauser effect Biochemistry Protein Structure Secondary Mice Structural Biology Genetics Animals Amino Acid Sequence Spectroscopy Molecular Biology Peptide sequence chemistry.chemical_classification Mice Inbred BALB C biology Chemistry Antibodies Monoclonal Cell Biology Peptide Fragments Transmembrane protein NMR N-terminus Bacteriorhodopsins biology.protein Oligopeptides |
| Zdroj: | FEBS Letters. (1-2):119-122 |
| ISSN: | 0014-5793 |
| DOI: | 10.1016/0014-5793(96)00094-4 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|