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Please use this identifier to cite or link to this item: https://olympias.lib.uoi.gr/jspui/handle/123456789/22312
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dc.contributor.authorWu, J.en
dc.contributor.authorFrillingos, S.en
dc.contributor.authorKaback, H. R.en
dc.date.accessioned2015-11-24T19:23:28Z-
dc.date.available2015-11-24T19:23:28Z-
dc.identifier.issn0006-2960-
dc.identifier.urihttps://olympias.lib.uoi.gr/jspui/handle/123456789/22312-
dc.rightsDefault Licence-
dc.subjectAmino Acid Sequenceen
dc.subjectAnilino Naphthalenesulfonatesen
dc.subjectCarbohydrate Sequenceen
dc.subjectCysteineen
dc.subjectEscherichia coli/*enzymology/geneticsen
dc.subject*Escherichia coli Proteinsen
dc.subjectEthylmaleimide/metabolismen
dc.subjectFluorescent Dyesen
dc.subjectKineticsen
dc.subjectMembrane Transport Proteins/biosynthesis/*chemistryen
dc.subjectMolecular Sequence Dataen
dc.subject*Monosaccharide Transport Proteinsen
dc.subjectMutagenesis, Site-Directeden
dc.subject*Protein Conformationen
dc.subject*Protein Structure, Secondaryen
dc.subjectPyrenesen
dc.subjectRecombinant Proteins/biosynthesis/chemistryen
dc.subjectSpectrometry, Fluorescenceen
dc.subjectSulfhydryl Reagentsen
dc.subject*Symportersen
dc.subjectThiogalactosidesen
dc.titleDynamics of lactose permease of Escherichia coli determined by site-directed chemical labeling and fluorescence spectroscopyen
heal.typejournalArticle-
heal.type.enJournal articleen
heal.type.elΆρθρο Περιοδικούel
heal.identifier.secondaryhttp://www.ncbi.nlm.nih.gov/pubmed/7599118-
heal.identifier.secondaryhttp://pubs.acs.org/doi/pdf/10.1021/bi00026a007-
heal.languageen-
heal.accesscampus-
heal.recordProviderΠανεπιστήμιο Ιωαννίνων. Σχολή Επιστημών Υγείας. Τμήμα Ιατρικήςel
heal.publicationDate1995-
heal.abstractMutants with a single Cys residue in place of Phe27, Pro28, Phe29, Phe30, or Pro31 at the periplasmic end of putative transmembrane helix I were used to study the interaction of lactose permease with ligand by site-directed chemical modification or fluorescence spectroscopy. With permease embedded in the native membrane, mutant Phe27-->Cys or Phe28-->Cys is readily labeled with [14C]-N-ethylmaleimide (NEM), while mutant Phe29-->Cys, Phe30-->Cys, or Phe31-->Cys reacts less effectively. beta,D-Galactopyranosyl 1-thio-beta,D-galactopyranoside (TDG) has little or no effect on the reactivity of Phe27-->Cys, Phe29-->Cys, or Phe30-->Cys permease. Remarkably, however, Pro31-->Cys permease which is essentially unreactive in the absence of ligand becomes highly reactive in the presence of TDG. Ligand also enhances the NEM reactivity of the mutant with Cys in place of Pro28 which is presumably on the same face of helix I as position 31. The five single-Cys mutants which also contain a biotin acceptor domain in the middle cytoplasmic loop were purified by monomeric avidin-affinity chromatography in dodecyl beta,D-maltoside and subjected to site-directed fluorescence spectroscopy. Mutants Phe27-->Cys, Phe29-->Cys, and Phe30-->Cys react rapidly with 2-(4'-maleimidylanilino)naphthalene-6-sulfonic acid (MIANS), and reactivity is not altered in the presence of TDG. In striking contrast, mutants Pro28-->Cys and Pro31-->Cys react extremely slowly with MIANS in the absent of ligand, and TDG dramatically enhances reactivity.(ABSTRACT TRUNCATED AT 250 WORDS)en
heal.journalNameBiochemistryen
heal.journalTypepeer-reviewed-
heal.fullTextAvailabilityTRUE-
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