Topography of surface-exposed amino acids in the membrane protein bacteriorhodopsin determined by proteolysis and micro-sequencing
- 1 January 1989
- journal article
- research article
- Published by Elsevier in Biochimica et Biophysica Acta (BBA) - Biomembranes
- Vol. 978 (2) , 231-240
- https://doi.org/10.1016/0005-2736(89)90120-x
Abstract
No abstract availableKeywords
This publication has 41 references indexed in Scilit:
- Extended N-terminal sequencing of proteins of archaebacterial ribosomes blotted from two-dimensional gels onto glass fiber and poly(vinylidene difluoride) membraneBiochemistry, 1988
- Two‐dimensional 1H‐NMR study of bacterioopsin‐(34–65)‐polypeptide conformationFEBS Letters, 1988
- pH dependence of bacteriorhodopsin thermal unfoldingBiochemistry, 1987
- Time‐course and stoichiometry of light‐induced proton release and uptake during the photocycle of bacteriorhodopsinFEBS Letters, 1986
- Stability of transmembrane regions in bacteriorhodopsin studied by progressive proteolysisThe Journal of Membrane Biology, 1985
- The antigenic structure and topography of bacteriorhodopsin in purple membranes as determined by interaction with monoclonal antibodiesFEBS Letters, 1985
- A probable linking sequence between two transmembrane components of bacteriorhodopsinFEBS Letters, 1981
- The structural basis of the functioning of bacteriorhodopsin: An overviewFEBS Letters, 1979
- Recent findings in the structure—functional characteristics of bacteriorhodopsinFEBS Letters, 1977
- The structure of the purple membrane from Halobacterium halobium: Analysis of the X-ray diffraction patternJournal of Molecular Biology, 1975