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Improved glucose-neopentyl glycol (GNG) amphiphiles for membrane protein solubilization and stabilization.

Authors
  • Cho, Kyung Ho
  • Bae, Hyoung Eun
  • Das, Manabendra
  • Gellman, Samuel H
  • Chae, Pil Seok
Type
Published Article
Journal
Chemistry - An Asian Journal
Publisher
Wiley (John Wiley & Sons)
Publication Date
Feb 01, 2014
Volume
9
Issue
2
Pages
632–638
Identifiers
DOI: 10.1002/asia.201301303
PMID: 24288216
Source
Medline
Keywords
License
Unknown

Abstract

Membrane proteins are inherently amphipathic and undergo dynamic conformational changes for proper function within native membranes. Maintaining the functional structures of these biomacromolecules in aqueous media is necessary for structural studies but difficult to achieve with currently available tools, thus necessitating the development of novel agents with favorable properties. This study introduces several new glucose-neopentyl glycol (GNG) amphiphiles and reveals some agents that display favorable behaviors for the solubilization and stabilization of a large, multi-subunit membrane protein assembly. Furthermore, a detergent structure-property relationship that could serve as a useful guideline for the design of novel amphiphiles is discussed.

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