Nuclear magnetic resonance analysis of Gd3+-induced perturbations in thymopoietin 32-36: a study of amide and aromatic proton resonances |
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Authors: | J B Vaughn R L Stephens R E Lenkinski G A Heavner G Goldstein N R Krishna |
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Affiliation: | 1. Comprehensive Cancer Center, U.S.A.;2. Departments of Biochemistry, University of Alabama, Birmingham, Alabama 35294 U.S.A.;3. Departments of Physics, University of Alabama, Birmingham, Alabama 35294 U.S.A.;4. Ortho Pharmaceutical Corporation, Raritan, New Jersey 08869 U.S.A. |
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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. |
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Keywords: | To whom correspondence should be addressed at the Comprehensive Cancer Center. |
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