Linked Life Data

9257702

Source:http://linkedlifedata.com/resource/pubmed/id/9257702

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pubmed-article:9257702pubmed:abstractTextInteraction of the Escherichia coli PapD chaperone with the synthetic peptide PapG308-314 (Thr-Met-Val-Leu-Ser-Phe-Pro), corresponding to the seven C-terminal residues of the PapG pilus subunit, was studied by transferred nuclear Overhauser effect (TRNOE) spectroscopy. The observation of cross-peaks corresponding to either intraresidue or sequential C(alpha)H/NH and C(beta)H/NH TRNOEs and the absence of sequential NH(i)/NH(i+1) TRNOEs indicate that the peptide binds to PapD in an extended conformation. In addition, line-broadening effects gave information of the peptide's mode of interaction with PapD. These observations were in excellent agreement with a recent crystal structure of a PapG peptide complexed with PapD.lld:pubmed
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pubmed-article:9257702pubmed:pagination115-20lld:pubmed
pubmed-article:9257702pubmed:dateRevised2006-11-15lld:pubmed
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pubmed-article:9257702pubmed:year1997lld:pubmed
pubmed-article:9257702pubmed:articleTitleTransferred nuclear Overhauser effect spectroscopy study of a peptide from the PapG pilus subunit bound by the Escherichia coli PapD chaperone.lld:pubmed
pubmed-article:9257702pubmed:affiliationPhysical Chemistry 2, Center for Chemistry and Chemical Engineering, Lund University, Sweden.lld:pubmed
pubmed-article:9257702pubmed:publicationTypeJournal Articlelld:pubmed
pubmed-article:9257702pubmed:publicationTypeResearch Support, Non-U.S. Gov'tlld:pubmed