MersV1, France, Analysis, bibRecord, 000272

Scanning transmission electron microscopy study of the molecular mass of amphipol/cytochrome b 6 f complexes

Identifieur interne : 000272 ( France/Analysis ); précédent : 000271; suivant : 000273

Scanning transmission electron microscopy study of the molecular mass of amphipol/cytochrome b 6 f complexes

Auteurs : C. Tribet [France] ; D. Mills [Allemagne] ; M. Haider [Allemagne] ; J. L. Popot [France]

Source :

Biochimie [ 0300-9084 ] ; 1998.

RBID : ISTEX:6C866A5375E3317494F2D755131C3F4F6729159B

English descriptors

Teeft :
- Aggregation, Aggregation state, Amac, Ammonium acetate, Ammonium buffer, Amphipol, Amphipol binding, Amphipol stock solution, Amphipols, Aqueous solutions, Biochemical composition, Centrifugation, Comparative study, Complexation, Conventional detergents, Cytochrome, Cytochrome complexes, Detergent solution, Detergent solutions, Electron microscopy, Excess amphipols, Excess lipids, Final complexes, Free amphipols, Heavy form, Hydroxylapatite column, Integral membrane proteins, Interesting perspectives, Light form, Lipid, Lipid binding, Liquid helium temperature, Mass analysis, Mass determination, Mass distribution, Membrane proteins, Molecular mass, Native form, Other hand, Polymer, Present address, Present article, Present study, Protease inhibitors, Purification protocols, Rate zonal centrifugation analysis, Rieske, Rieske protein, Rieske subunit, Scanning transmission electron microscopy, Stock solution, Subunit, Subunit petl, Sucrose, Sucrose gradient, Sucrose gradients, Tobacco mosaic virus, Unpublished observations.

Abstract

Abstract: The composition and mass of complexes between Chlamydomonas reinhardtii cytochrome b6f and low molecular mass amphipathic polymers (‘amphipols’) have been studied using biochemical analysis and scanning transmission electron microscopy at liquid helium temperature (cryo-STEM). Cytochrome b6f was trapped by amphipols either under its native 14-meric state or as a delipidated, lighter form. A good consistency was observed between the masses of either form calculated from their biochemical composition and those determined by cryo-STEM. These data show that association with amphipols preserved the original aggregation state of the protein in detergent solution. Complexation with amphipols appears to facilitate preparation of the samples and mass determination by cryo-STEM as compared to conventional solubilization with detergents.

Url:

https://api.istex.fr/ark:/67375/6H6-G4CKWCNR-H/fulltext.pdf

DOI: 10.1016/S0300-9084(00)80014-0

Affiliations:

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ISTEX:6C866A5375E3317494F2D755131C3F4F6729159B

Le document en format XML

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<term>Ammonium buffer</term>
<term>Amphipol</term>
<term>Amphipol binding</term>
<term>Amphipol stock solution</term>
<term>Amphipols</term>
<term>Aqueous solutions</term>
<term>Biochemical composition</term>
<term>Centrifugation</term>
<term>Comparative study</term>
<term>Complexation</term>
<term>Conventional detergents</term>
<term>Cytochrome</term>
<term>Cytochrome complexes</term>
<term>Detergent solution</term>
<term>Detergent solutions</term>
<term>Electron microscopy</term>
<term>Excess amphipols</term>
<term>Excess lipids</term>
<term>Final complexes</term>
<term>Free amphipols</term>
<term>Heavy form</term>
<term>Hydroxylapatite column</term>
<term>Integral membrane proteins</term>
<term>Interesting perspectives</term>
<term>Light form</term>
<term>Lipid</term>
<term>Lipid binding</term>
<term>Liquid helium temperature</term>
<term>Mass analysis</term>
<term>Mass determination</term>
<term>Mass distribution</term>
<term>Membrane proteins</term>
<term>Molecular mass</term>
<term>Native form</term>
<term>Other hand</term>
<term>Polymer</term>
<term>Present address</term>
<term>Present article</term>
<term>Present study</term>
<term>Protease inhibitors</term>
<term>Purification protocols</term>
<term>Rate zonal centrifugation analysis</term>
<term>Rieske</term>
<term>Rieske protein</term>
<term>Rieske subunit</term>
<term>Scanning transmission electron microscopy</term>
<term>Stock solution</term>
<term>Subunit</term>
<term>Subunit petl</term>
<term>Sucrose</term>
<term>Sucrose gradient</term>
<term>Sucrose gradients</term>
<term>Tobacco mosaic virus</term>
<term>Unpublished observations</term>
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<front><div type="abstract" xml:lang="en">Abstract: The composition and mass of complexes between Chlamydomonas reinhardtii cytochrome b6f and low molecular mass amphipathic polymers (‘amphipols’) have been studied using biochemical analysis and scanning transmission electron microscopy at liquid helium temperature (cryo-STEM). Cytochrome b6f was trapped by amphipols either under its native 14-meric state or as a delipidated, lighter form. A good consistency was observed between the masses of either form calculated from their biochemical composition and those determined by cryo-STEM. These data show that association with amphipols preserved the original aggregation state of the protein in detergent solution. Complexation with amphipols appears to facilitate preparation of the samples and mass determination by cryo-STEM as compared to conventional solubilization with detergents.</div>
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Scanning transmission electron microscopy study of the molecular mass of amphipol/cytochrome b 6 f complexes

Scanning transmission electron microscopy study of the molecular mass of amphipol/cytochrome b 6 f complexes

Source :

English descriptors

Abstract

Links toward previous steps (curation, corpus...)

Links to Exploration step

Le document en format XML

Pour manipuler ce document sous Unix (Dilib)

Pour mettre un lien sur cette page dans le réseau Wicri