Lipid-protein interactions in the purple membrane: structural specificity within the hydrophobic domain
| Autor: | Veronique Pomerleau, Erik Harvey-Girard, Frangois Boucher |
|---|---|
| Rok vydání: | 1995 |
| Předmět: |
Halobacterium salinarum
Biophysics Bacteriorhodopsin Biochemistry Protein–protein interaction Pigment Structure-Activity Relationship Protein structure Purple Membrane Organic chemistry Alkyl Phospholipids chemistry.chemical_classification biology Vesicle Cell Biology Chromophore Hydrogen-Ion Concentration Membrane chemistry Spectrophotometry Methyl-substituted alkyl chain visual_art Bacteriorhodopsins visual_art.visual_art_medium biology.protein lipids (amino acids peptides and proteins) Lipid-protein interaction |
| Zdroj: | Biochimica et biophysica acta. 1234(2) |
| ISSN: | 0006-3002 |
| Popis: | In the absence of native-like interactions between bacteriorhodopsin and its neighbouring lipids, the pigment chromophore is reversibly titrated from its purple 570 nm form to a blue-shifted 480 nm form in the moderately alkaline pH range. Quantitation of this acid-base chromophore equilibrium in vesicles prepared from modified lipid mixtures shows that it is absent under conditions where bacteriorhodopsin is allowed to interact with methyl-substituted alkyl chains. The peculiar homogeneous structure of purple membrane alkyl chain lipids is thus likely to be an essential requirement for maintenance of the native bacteriorhodopsin structure over a wide pH range. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|