By a News Reporter-Staff News Editor at Life Science Weekly -- Data detailed on Membrane Proteins have been presented. According to news originating from Pasadena, California, by NewsRx correspondents, research stated, "We demonstrate that membrane proteins and phospholipids can self-assemble into polyhedral arrangements suitable for structural analysis. Using the Escherichia coli mechanosensitive channel of small conductance (MscS) as a model protein, we prepared membrane protein polyhedral nanoparticles (MPPNs) with uniform radii of similar to 20 nm."
Our news journalists obtained a quote from the research from the California Institute of Technology, "Electron cryotomographic analysis established that these MPPNs contain 24 MscS heptamers related by octahedral symmetry. Subsequent single-particle electron cryomicroscopy yielded a reconstruction at similar to 1-nm resolution, revealing a conformation closely resembling the nonconducting state. The generality of this approach has been addressed by the successful preparation of MPPNs for two unrelated proteins, the mechanosensitive channel of large conductance and the connexon Cx26, using a recently devised microfluidics-based free interface diffusion system."
According to the news editors, the research concluded: "MPPNs provide not only a starting point for the structural analysis of membrane proteins in a phospholipid environment, but their closed surfaces should facilitate studies in the presence of physiological transmembrane gradients, in addition to potential applications as drug delivery carriers or as templates for inorganic nanoparticle formation."
For more information on this research see: Self-assembled lipid and membrane protein polyhedral nanoparticles. Proceedings of the National Academy of Sciences of the United States of America, 2014;111(2):670-674. Proceedings of the National Academy of Sciences of the United States of America can be contacted at: Natl Acad Sciences, 2101 Constitution Ave NW, Washington, DC 20418, USA. (National Academy of Sciences - www.nasonline.org/; Proceedings of the National Academy of Sciences of the United States of America - www.nasonline.org/publications/pnas/)
The news correspondents report that additional information may be obtained from T. Basta, California Institute of Technology, Div Chem & Chem Engn, Pasadena, CA 91125, United States. Additional authors for this research include H.J. Wu, M.K. Morphew, J. Lee, N. Ghosh, J. Lai, J.M. Heumann, K. Wang, Y.C. Lee, D.C. Rees and M.H.B. Stowell (see also Membrane Proteins).
Keywords for this news article include: Pasadena, Peptides, California, Amino Acids, Nanoparticle, United States, Nanotechnology, Membrane Proteins, Emerging Technologies, North and Central America
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