By Arun K. Shukla

Membrane Proteins - Engineering, Purification and Crystallization, a quantity of Methods In Enzymology, encompasses chapters from the top specialists within the zone of membrane protein biology. The chapters supply a short review of the themes lined and likewise define step by step protocol for the viewers. Illustrations and case instance photographs are incorporated anyplace acceptable to assist the readers comprehend the schematics and normal experimental outlines.

  • Volume of Methods In Enzymology
  • Contains a set of a various array of subject matters within the sector of membrane protein biology starting from recombinant expression, isolation, sensible characterization, biophysical experiences and crystallization

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Extra resources for Membrane proteins. Volume 557, Engineering, purification and crystallization

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Expression Screening and Functional Assays 6. Results for the Yeast α-Factor Receptor Ste2p Acknowledgments References 28 30 32 32 33 33 33 33 34 37 39 40 40 Abstract Determination of high-resolution, three-dimensional structures of transmembrane proteins (TMPs) has, in many cases, only been accomplished through the use of stabilized variant forms of the proteins being studied. For the important G protein-coupled receptor superfamily, this has most often been achieved by inserting a stable soluble protein, such as T4 lysozyme (T4L), in an internal loop of a receptor.

2013). This is an important point to be considered in view of the fact that GPCR constructs used for crystallography involve truncations of the C-terminal to remove regions presumed to have excess flexibility. The most active T4L-containing variants of full-length Ste2p contained the inserted protein flanked by nearly complete IC3 loop sequences that were duplicated at both the N- and C-terminal sides of the insertion. We confirmed that duplication of the IC3 loop, even in the absence of any inserted T4L, is not detrimental to receptor signaling.

Results for the Yeast α-Factor Receptor Ste2p Acknowledgments References 28 30 32 32 33 33 33 33 34 37 39 40 40 Abstract Determination of high-resolution, three-dimensional structures of transmembrane proteins (TMPs) has, in many cases, only been accomplished through the use of stabilized variant forms of the proteins being studied. For the important G protein-coupled receptor superfamily, this has most often been achieved by inserting a stable soluble protein, such as T4 lysozyme (T4L), in an internal loop of a receptor.

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