| Literature DB >> 27437691 |
Ida Louise Jørgensen1, Gerdi Christine Kemmer2, Thomas Günther Pomorski3,4.
Abstract
Studying membrane proteins at the molecular level represents a major challenge in biochemistry due to the complexity of the membrane in which they are embedded. As an important step towards a detailed understanding of their action and molecular functioning, current studies focus on membrane proteins reconstituted into artificial lipid environments. Such reconstituted systems allow for a more flexible choice of biochemical, biophysical, and microscopy techniques for characterizing the proteins. This review gives an overview of the methods currently available for reconstituting membrane proteins in a functional state into giant unilamellar vesicles, and discusses some key methods to verify successful reconstitution.Entities:
Keywords: Electroformation; Liposome; Peptide-induced fusion; Reconstitution; Vesicle
Mesh:
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Year: 2016 PMID: 27437691 DOI: 10.1007/s00249-016-1155-9
Source DB: PubMed Journal: Eur Biophys J ISSN: 0175-7571 Impact factor: 1.733