title: Topology determination of untagged membrane proteins.
abstract: The topology of integral membrane proteins with a weak topological tendency can be influenced when fused to tags, such as these used for topological determination or protein purification. Here, we describe a technique for topology determination of an untagged membrane protein. This technique, optimized for bacterial cells, allows the visualization of the protein in the native environment and incorporates the substituted-cysteine accessibility method.
authors.affiliation: Department of Biological Chemistry, Hebrew University of Jerusalem, Jerusalem, Israel.
authors.forename: Iris
authors.initials: I
authors.lastname: Nasie
authors.forename: Sonia
authors.initials: S
authors.lastname: Steiner-Mordoch
authors.forename: Shimon
authors.initials: S
authors.lastname: Schuldiner
mesh_terms: D017920:Antiporters / Q000737:chemistry; D003545:Cysteine / Q000737:chemistry / Q000378:metabolism; D029968:Escherichia coli Proteins / Q000737:chemistry; D006358:Hot Temperature; D008565:Membrane Proteins / Q000737:chemistry* / Q000378:metabolism; D008715:Methionine / Q000737:chemistry; D011489:Protein Denaturation; D040901:Proteomics / Q000379:methods; D013194:Staining and Labeling; D013462:Sulfur Radioisotopes / Q000737:chemistry
chemical_list: D017920:Antiporters; D029968:Escherichia coli Proteins; D008565:Membrane Proteins; D013462:Sulfur Radioisotopes; C075436:EmrE protein, E coli; D008715:Methionine; D003545:Cysteine