Studying the spatial organization of membrane proteins by means of tritium stratigraphy: bacteriorhodopsin in purple membrane-Reference-Cited by-同舟云学术

Studying the spatial organization of membrane proteins by means of tritium stratigraphy: bacteriorhodopsin in purple membrane

Published:2002-05 Issue:1-2 Volume:56 Page:147-149
ISSN:1567-5394
Container-title:Bioelectrochemistry
language:en
Short-container-title:Bioelectrochemistry

Author:

Shishkov A.V.,Ksenofontov A.L.,Bogacheva E.N.,Kordyukova L.V.,Badun G.A.,Alekseevsky A.V.,Tsetlin V.I.,Baratova L.A.

Publisher

Elsevier BV

Subject

Electrochemistry,Physical and Theoretical Chemistry,General Medicine,Biophysics

Reference8 articles.

1. Tritium thermal activation study of bacteriorhodopsin topography;Tsetlin;Eur. J. Biochem.,1988

2. The use of thermally activated tritium atoms for structural–biological investigations: the topography of the TMV protein-accessible surface of the virus;Goldanskii;J. Mol. Biol.,1988

3. Lipid patches in membrane protein oligomers: crystal structure of the bacteriorhodopsin–lipid complex;Essen;Proc. Natl. Acad. Sci. U. S. A.,1998

4. The in situ spatial arrangement of the influenza A virus matrix protein M1 assessed by tritium bombardment;Shishkov;Proc. Natl. Acad. Sci.,1999

5. The concept of the “accessible surface” of the protein within the framework of tritium planigraphy: experiment and calculation;Bogacheva;Mol. Biol.,1994

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