The influence of heptane-1,2,3-triol on the size and shape of LDAO micelles Implications for the crystallisation of membrane proteins
Autor: | Peter Timmins, Wolfram Welte, Jürgen Hauk, Thomas Wacker |
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Rok vydání: | 1991 |
Předmět: |
Surfactant micelles
Small angle neutron scattering Biophysics Membrane protein crystallization Biochemistry Micelle law.invention chemistry.chemical_compound X-Ray Diffraction Pulmonary surfactant Structural Biology law Amphiphile Genetics Organic chemistry Mixed micelles Crystallization Molecular Biology Micelles Neutrons Heptane Membrane Proteins Cell Biology Small-angle neutron scattering Amine oxide Small amphiphiles chemistry Chemical engineering Particle size Fatty Alcohols Dimethylamines |
Zdroj: | FEBS Letters. 280:115-120 |
ISSN: | 0014-5793 |
DOI: | 10.1016/0014-5793(91)80217-q |
Popis: | The presence of small amphiphiles has been found to be necessary in the crystallization of several membrane-protein surfactant complexes. It has been suggested that the role of the small amphiphile may be to reduce the size of the surfactant belt around the protein, making the formation of crystals easier. Thus far it was not known if this would involve changes in micellar size in general or whether the small amphiphile would merely replace LDAO during crystal growth. In the present study we have used small angle neutron scattering to study mixed micelles of lauryldimethyl amine oxide (LDAO; hydrogenated and deuterated) and heptane-1,2,3-triol (HP). Our results show that with increasing overall HP concentrations mixed LDAO/HP micelles of decreasing mass and radius are formed. The composition of these micelles has been determined. HP thus may decrease the size of the surfactant belt around a protein before crystallisation by insertion into a host micelle. As HP is a ‘small amphiphile’ compared to the surfactants used for solubilization of membrane proteins, the curvature of the host micelle will be increased by its insertion. |
Databáze: | OpenAIRE |
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