A Lipidic-Sponge Phase Screen for Membrane Protein Crystallization

jerry submitted, created time 5 months 3 weeks (www.structure.org)

A major current deficit in structural biology is the lack of high-resolution structures of eukaryotic membrane proteins, many of which are key drug targets for the treatment of disease. Numerous eukaryotic membrane proteins require specific lipids for their stability and activity, and efforts to crystallize and solve the structures of membrane proteins that do not address the issue of lipids frequently end in failure rather than success. To help address this problem, they have developed a sparse matrix crystallization screen consisting of 48 lipidic-sponge phase conditions

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The role of hydrophobic interactions in positioning of peripheral proteins in membranes

DanyC submitted, created time 1 year 6 months (www.biomedcentral.com)

“Positions of diverse peripheral proteins and peptides in the lipid bilayer can be accurately predicted using their 3D structures that represent a proper membrane-bound conformation and oligomeric state, and have membrane binding elements present. The success of the implicit solvation model suggests that hydrophobic interactions are usually sufficient to determine the spatial position of a protein in the membrane, even when electrostatic interactions or specific binding of lipids are substantial

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Homologous high-throughput expression and purification of highly conserved E. coli Proteins

annatto submitted, created time 1 year 6 months (www.microbialcellfactories.com)

"As a standardized procedure, genes were PCR amplified and cloned into the expression vector pQTEV2 in order to express proteins N-terminally fused to a seven-histidine-tag. Initial small-scale expression and purification under native conditions by metal chelate affinity chromatography indicated that the vast majority of target proteins were purified in high yields

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A rational route to probing membrane proteins

annatto submitted, created time 1 year 7 months (genomebiology.com)

"A recent report describes the design of short peptides that bind specifically to transmembrane regions of integrins, providing an exciting tool for probing the biology of membrane proteins."

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