| Autor: |
Yu SM; Department of Chemistry, University of Wisconsin, Madison 53706, USA., McQuade DT, Quinn MA, Hackenberger CP, Krebs MP, Polans AS, Gellman SH |
| Jazyk: |
angličtina |
| Zdroj: |
Protein science : a publication of the Protein Society [Protein Sci] 2000 Dec; Vol. 9 (12), pp. 2518-27. |
| DOI: |
10.1110/ps.9.12.2518 |
| Abstrakt: |
Intrinsic membrane proteins represent a large fraction of the proteins produced by living organisms and perform many crucial functions. Structural and functional characterization of membrane proteins generally requires that they be extracted from the native lipid bilayer and solubilized with a small synthetic amphiphile, for example, a detergent. We describe the development of a small molecule with a distinctive amphiphilic architecture, a "tripod amphiphile," that solubilizes both bacteriorhodopsin (BR) and bovine rhodopsin (Rho). The polar portion of this amphiphile contains an amide and an amine-oxide; small variations in this polar segment are found to have profound effects on protein solubilization properties. The optimal tripod amphiphile extracts both BR and Rho from the native membrane environments and maintains each protein in a monomeric native-like form for several weeks after delipidation. Tripod amphiphiles are designed to display greater conformational rigidity than conventional detergents, with the long-range goal of promoting membrane protein crystallization. The results reported here represent an important step toward that ultimate goal. |
| Databáze: |
MEDLINE |
| Externí odkaz: |
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