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10.1021/jacs.5b13426 http://scihub22266oqcxt.onion/10.1021/jacs.5b13426 C5480290!5480290!26918528     free     free     free Warning: file_get_contents(https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pubmed&id=26918528&cmd=llinks): Failed to open stream: HTTP request failed! 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Probing Polytopic Membrane Protein - Substrate Interactions by Luminescence Resonance Energy Transfer |pdf=|usr=}}{{26918528}} gab.com Text Probing Polytopic Membrane Protein - Substrate Interactions by Luminescence Resonance Energy Transfer JO: J Am Chem Soc http://www.kidney.de/pget.php?&tw=1&pmid=26918528 #FOAvip Integral membrane proteins play essential roles in all living systems; however, major technical hurdles challenge analyses of this class of proteins. Biophysical approaches that provide structural information to complement and leverage experimentally-determined and computationally-predicted structures are urgently needed. Herein we present the application of luminescence resonance energy transfer (LRET) for investigating the interactions of the polytopic membrane-bound oligosaccharyl transferases (OTases) with partner substrates. Monomeric OTases, such as the PglBs from Campylobacter jejuni and C. lari catalyze transfer of glycans from membrane?associated undecaprenol diphosphate-linked substrates to proteins in the bacterial periplasm. LRET-based distance measurements are enabled by the inclusion of an encoded N-terminal lanthanide-binding tags (LBTs), and LRET between the luminescent (LBT)-Tb3+ donor complex and fluorescently-labeled peptide and glycan substrates, provides discrete distance measurements across the span of the membrane. LRET-based measurements of detergent-solubilized PglB from C. lari allowed direct comparison with the distances based on the previously reported the C. lari PglB crystal structure, thereby validating the approach in a defined system. Distance measurements between peptide and glycan substrates and the C. jejuni PglB offer new experimental information on substrate binding to the related, but structurally uncharacterized, OTase. Twit Text FOAVip Probing Polytopic Membrane Protein - Substrate Interactions by Luminescence Resonance Energy Transfer ????J Am Chem Soc http://www.kidney.de/pget.php?&tw=1&pmid=26918528 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=26918528 #FOAvip English Wikipedia <ref>{{Cite pmid|26918528}}</ref> Probing Polytopic Membrane Protein - Substrate Interactions by Luminescence Resonance Energy Transfer #MMPMID26918528 Musial-Siwek M; Jaffee MB; Imperiali B J Am Chem Soc 2016[Mar]; 138 (11): 3806-12 PMID26918528show ga Integral membrane proteins play essential roles in all living systems; however, major technical hurdles challenge analyses of this class of proteins. Biophysical approaches that provide structural information to complement and leverage experimentally-determined and computationally-predicted structures are urgently needed. Herein we present the application of luminescence resonance energy transfer (LRET) for investigating the interactions of the polytopic membrane-bound oligosaccharyl transferases (OTases) with partner substrates. Monomeric OTases, such as the PglBs from Campylobacter jejuni and C. lari catalyze transfer of glycans from membrane?associated undecaprenol diphosphate-linked substrates to proteins in the bacterial periplasm. LRET-based distance measurements are enabled by the inclusion of an encoded N-terminal lanthanide-binding tags (LBTs), and LRET between the luminescent (LBT)-Tb3+ donor complex and fluorescently-labeled peptide and glycan substrates, provides discrete distance measurements across the span of the membrane. LRET-based measurements of detergent-solubilized PglB from C. lari allowed direct comparison with the distances based on the previously reported the C. lari PglB crystal structure, thereby validating the approach in a defined system. Distance measurements between peptide and glycan substrates and the C. jejuni PglB offer new experimental information on substrate binding to the related, but structurally uncharacterized, OTase. äProbing Polytopic Membrane Protein - Substrate Interactions by Lumines(epmc).pdf DeepDyve Pubget Overpricing