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http://purl.uniprot.org/citations/12475238http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/12475238http://www.w3.org/2000/01/rdf-schema#comment"The unique trypsin cleavable site of NhaA, the Na(+)/H(+) antiporter of Escherichia coli, was exploited to detect a change in mobility of cross-linked products of NhaA by polyacrylamide gel electrophoresis. Double-Cys replacements were introduced into loops, one on each side of the trypsin cleavage site (Lys 249). The proximity of paired Cys residues was assessed by disulfide cross-linking of the two tryptic fragments, using three homobifunctional cross-linking agents: 1,6-bis(maleimido)hexane (BMH), N,N'-o-phenylenedimaleimide (o-PDM), and N,N'-p-phenylenedimaleimide (p-PDM). The interloop cross-linking was found to be very specific, indicating that the loops are not merely random coils that interact randomly. In the periplasmic side of NhaA, two patterns of cross-linking are observed: (a) all three cross-linking reagents cross-link very efficiently between the double-Cys replacements A118C/S286C, N177C/S352C, and H225C/S352C; (b) only BMH cross-links the double-Cys replacements A118C/S352C, N177C/S286C, and H225C/S286C. In the cytoplasmic side of NhaA, three patterns of cross-linking are observed: (a) all three cross-linking reagents cross-link very efficiently the pairs of Cys replacements L4C/E252C, S146C/L316C, S146C/R383C, and E241C/E252C; (b) BMH and p-PDM cross-link efficiently the pairs of Cys replacements S87C/E252C, S87C/L316C, and S146C/E252C; (c) none of the reagents cross-links the double-Cys replacements L4C/L316C, L4C/R383C, S87C/R383C, A202C/E252C, A202C/L316C, A202C/R383C, E241C/L316C, and E241C/R383C. The data reveal that the N-terminus and loop VIII-IX that have previously been shown to change conformation with pH are in close proximity within the NhaA protein. The data also suggest close proximity between N-terminal and C-terminal helices at both the cytoplasmic and the periplasmic face of NhaA."xsd:string
http://purl.uniprot.org/citations/12475238http://purl.org/dc/terms/identifier"doi:10.1021/bi0261342"xsd:string
http://purl.uniprot.org/citations/12475238http://purl.uniprot.org/core/author"Padan E."xsd:string
http://purl.uniprot.org/citations/12475238http://purl.uniprot.org/core/author"Rimon A."xsd:string
http://purl.uniprot.org/citations/12475238http://purl.uniprot.org/core/author"Tzubery T."xsd:string
http://purl.uniprot.org/citations/12475238http://purl.uniprot.org/core/author"Galili L."xsd:string
http://purl.uniprot.org/citations/12475238http://purl.uniprot.org/core/date"2002"xsd:gYear
http://purl.uniprot.org/citations/12475238http://purl.uniprot.org/core/name"Biochemistry"xsd:string
http://purl.uniprot.org/citations/12475238http://purl.uniprot.org/core/pages"14897-14905"xsd:string
http://purl.uniprot.org/citations/12475238http://purl.uniprot.org/core/title"Proximity of cytoplasmic and periplasmic loops in NhaA Na+/H+ antiporter of Escherichia coli as determined by site-directed thiol cross-linking."xsd:string
http://purl.uniprot.org/citations/12475238http://purl.uniprot.org/core/volume"41"xsd:string
http://purl.uniprot.org/citations/12475238http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/12475238
http://purl.uniprot.org/citations/12475238http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/12475238
http://purl.uniprot.org/uniprot/#_P13738-mappedCitation-12475238http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/12475238
http://purl.uniprot.org/uniprot/P13738http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/12475238