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A class of rigid linker-bearing glucosides for membrane protein structural study
Sadaf, A.,Mortensen, J.,Capaldi, S.,Tikhonova, E.,Hariharan, P.,Ribeiro, O.,Loland, C.,Guan, L.,Byrne, B.,Chae, P. THE ROYAL SOCIETY OF CHEMISTRY 2016 Chemical Science Vol.7 No.3
<P>Membrane proteins are amphipathic bio-macromolecules incompatible with the polar environments of aqueous media. Conventional detergents encapsulate the hydrophobic surfaces of membrane proteins allowing them to exist in aqueous solution. Membrane proteins stabilized by detergent micelles are used for structural and functional analysis. Despite the availability of a large number of detergents, only a few agents are sufficiently effective at maintaining the integrity of membrane proteins to allow successful crystallization. In the present study, we describe a novel class of synthetic amphiphiles with a branched tail group and a triglucoside head group. These head and tail groups were connected via an amide or ether linkage by using a tris(hydroxylmethyl) aminomethane (TRIS) or neopentyl glycol (NPG) linker to produce TRIS-derived triglucosides (TDTs) and NPG-derived triglucosides (NDTs), respectively. Members of this class conferred enhanced stability on target membrane proteins compared to conventional detergents. Because of straightforward synthesis of the novel agents and their favourable effects on a range of membrane proteins, these agents should be of wide applicability to membrane protein science.</P>
Uniform nomenclature for the mitochondrial contact site and cristae organizing system
Pfanner, Nikolaus,van der Laan, Martin,Amati, Paolo,Capaldi, Roderick A.,Caudy, Amy A.,Chacinska, Agnieszka,Darshi, Manjula,Deckers, Markus,Hoppins, Suzanne,Icho, Tateo,Jakobs, Stefan,Ji, Jianguo,Kozj The Rockefeller University Press 2014 The Journal of cell biology Vol.204 No.7
<P>The mitochondrial inner membrane contains a large protein complex that functions in inner membrane organization and formation of membrane contact sites. The complex was variably named the mitochondrial contact site complex, mitochondrial inner membrane organizing system, mitochondrial organizing structure, or Mitofilin/Fcj1 complex. To facilitate future studies, we propose to unify the nomenclature and term the complex “mitochondrial contact site and cristae organizing system” and its subunits Mic10 to Mic60.</P>
Glucose-Neopentyl Glycol (GNG) amphiphiles for membrane protein study
Chae, Pil Seok,Rana, Rohini R.,Gotfryd, Kamil,Rasmussen, Søren G. F.,Kruse, Andrew C.,Cho, Kyung Ho,Capaldi, Stefano,Carlsson, Emil,Kobilka, Brian,Loland, Claus J.,Gether, Ulrik,Banerjee, Surajit,Byrn The Royal Society of Chemistry 2013 Chemical communications Vol.49 No.23
<P>The development of a new class of surfactants for membrane protein manipulation, “GNG amphiphiles”, is reported. These amphiphiles display promising behavior for membrane proteins, as demonstrated recently by the high resolution structure of a sodium-pumping pyrophosphatase reported by Kellosalo <I>et al.</I> (<I>Science</I>, 2012, 337, 473).</P> <P>Graphic Abstract</P><P>A new class of surfactants, the GNGs, tends to form small protein–detergent complexes, which may be favorable for crystallization. <IMG SRC='http://pubs.rsc.org/services/images/RSCpubs.ePlatform.Service.FreeContent.ImageService.svc/ImageService/image/GA?id=c2cc36844g'> </P>