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Folding and stability of integral membrane proteins in amphipols

期刊

ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS
卷 564, 期 -, 页码 327-343

出版社

ELSEVIER SCIENCE INC
DOI: 10.1016/j.abb.2014.10.013

关键词

Membrane protein; Folding; Amphipols; Kinetics; Thermodynamic stability; Outer membrane proteins; Bacteriorhodopsin; G protein-coupled receptors; A8-35

资金

  1. Deutsche Forschungsgemeinschaft
  2. University of Konstanz
  3. University of Kassel
  4. French Centre National de la Recherche Scientifique, University Paris-7 Denis Diderot
  5. Human Frontier Scientific Program Organization
  6. European Community
  7. Agence Nationale pour la Recherche
  8. US National Institutes of Health

向作者/读者索取更多资源

Amphipols (APols) are a family of amphipathic polymers designed to keep transmembrane proteins (TMPs) soluble in aqueous solutions in the absence of detergent. APols have proven remarkably efficient at (i) stabilizing TMPs, as compared to detergent solutions, and (ii) folding them from a denatured state to a native, functional one. The underlying physical chemical mechanisms are discussed. (C) 2014 Elsevier Inc. All rights reserved.

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