Nuclear magnetic resonance analysis of Gd3+-induced perturbations in thymopoietin32-36: A study of amide and aromatic proton resonances

Joseph B. Vaughn, Richard L. Stephens, Robert E. Lenkinski, George A. Heavner, Gideon Goldstein, N. Rama Krishna

Research output: Contribution to journalArticle

7 Scopus citations

Abstract

The Gd3+-induced perturbations in the NMR spectra of a cell differentiating peptide fragment, ArgLysAspValTyr (TP5), have been examined. This pentapeptide fragment retains the selective T-cell differentiating activity of its parent polypeptide thymic hormone, thymopoietin. The observed relaxation enhancements induced by Gd3+ have been analyzed to determine the relative and absolute amide and aromatic proton-Gd3+ distances. The data are compatible with a bidentate model, in which both the aspartyl and tyrosyl carboxylates bind the metal ion simultaneously in a chelate fashion, being the dominant conformer. From these studies a picture of the conformation of Ln3+ complexes of TP5 begins to emerge.

Original languageEnglish (US)
Pages (from-to)468-472
Number of pages5
JournalArchives of Biochemistry and Biophysics
Volume217
Issue number2
DOIs
StatePublished - Sep 1982

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology

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