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Hemifluorinated maltose-neopentyl glycol (HF-MNG) amphiphiles for membrane protein stabilisation.

Identifieur interne : 000583 ( Main/Exploration ); précédent : 000582; suivant : 000584

Hemifluorinated maltose-neopentyl glycol (HF-MNG) amphiphiles for membrane protein stabilisation.

Auteurs : Kyung Ho Cho [Corée du Sud] ; Bernadette Byrne ; Pil Seok Chae

Source :

RBID : pubmed:23401323

Mots-clés :

Abstract

SOAP OPERA: Fluorinated amphiphile F4-MNG confers greater stability on Rhodobacter capsulatus superassembly relative to conventional detergents and nonfluorinated MNGs. Such amphiphiles are attractive as tools for membrane science because of their ease of preparation and structure variation.


DOI: 10.1002/cbic.201200759


Affiliations:


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Le document en format XML

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<name sortKey="Cho, Kyung Ho" sort="Cho, Kyung Ho" uniqKey="Cho K" first="Kyung Ho" last="Cho">Kyung Ho Cho</name>
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<nlm:affiliation>Department of Bionano Engineering, Hanyang University, 55 Hanyangdaehak-ro, Sangnok-gu, Ansan, 426-791, Korea.</nlm:affiliation>
<country xml:lang="fr">Corée du Sud</country>
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<name sortKey="Byrne, Bernadette" sort="Byrne, Bernadette" uniqKey="Byrne B" first="Bernadette" last="Byrne">Bernadette Byrne</name>
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<name sortKey="Chae, Pil Seok" sort="Chae, Pil Seok" uniqKey="Chae P" first="Pil Seok" last="Chae">Pil Seok Chae</name>
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<title level="j">Chembiochem : a European journal of chemical biology</title>
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<term>Bacterial Proteins (chemistry)</term>
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<term>Rhodobacter capsulatus</term>
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<div type="abstract" xml:lang="en">SOAP OPERA: Fluorinated amphiphile F4-MNG confers greater stability on Rhodobacter capsulatus superassembly relative to conventional detergents and nonfluorinated MNGs. Such amphiphiles are attractive as tools for membrane science because of their ease of preparation and structure variation.</div>
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