| Autor: |
Pashkov VS; Shemyakin-Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, ul. Miklukho-Maklaya 16/10, GSP Moscow, 117997 Russia. pavs@nmr.ru, Mareeva TIu, Balashova TA, Vychalkovskiĭ AA, Samokhvalova LV, Baĭdakova LK, Rodionov IL, Nesmeianov VA |
| Jazyk: |
ruština |
| Zdroj: |
Bioorganicheskaia khimiia [Bioorg Khim] 2002 Mar-Apr; Vol. 28 (2), pp. 109-17. |
| DOI: |
10.1023/a:1015061222433 |
| Abstrakt: |
Effect of the monoclonal antibody (MAb) 5B6 produced to the solubilized preparation of bacteriorhodopsin on the protein photocycle was studied to examine conformational rearrangements on the surface of functioning bacteriorhodopsin molecule. Using the methods of solid phase enzyme immunoassay, peptide phage display, and 1H NMR spectroscopy, we demonstrated that the epitope recognized by MAb 5B6 is the Val69-Pro-Phe-Gly72 fragment of the protein, with the aromatic ring of Phe71 and the methyl groups of Val69 participating in the binding. MAb 5B6 exerted no significant effect on the photocycle of bacteriorhodopsin solubilized in Triton X-100 at pH 6.2 and 7.4, which suggested that, when functioning, bacteriorhodopsin retains the conformation and position of its Val69-Pro-Phe-Gly72 fragment. |
| Databáze: |
MEDLINE |
| Externí odkaz: |
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