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Transferred nuclear Overhauser effect spectroscopy study of a peptide from the PapG pilus subunit bound by the Escherichia coli PapD chaperone
Author(s) -
Walse Björn,
Kihlberg Jan,
Flemmer Karlsson Katarina,
Wahlund Karl-Gustav,
Pinkner Jerome S,
Hultgren Scott J,
Drakenberg Torbjörn
Publication year - 1997
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(97)00759-x
Subject(s) - pilus , peptide , chaperone (clinical) , escherichia coli , protein subunit , chemistry , nuclear overhauser effect , crystallography , spectroscopy , nuclear magnetic resonance spectroscopy , biophysics , biochemistry , biology , stereochemistry , medicine , physics , pathology , quantum mechanics , gene
Interaction 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 α H/NH and C β 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.