TY - JOUR
T1 - Nuclear magnetic resonance analysis of Gd3+-induced perturbations in thymopoietin32-36
T2 - A study of amide and aromatic proton resonances
AU - Vaughn, Joseph B.
AU - Stephens, Richard L.
AU - Lenkinski, Robert E.
AU - Heavner, George A.
AU - Goldstein, Gideon
AU - Krishna, N. Rama
N1 - Funding Information:
Support of this work by U. S. Public Health Service Grant GM-26219 (N.R.K.), and Postdoctoral Fellowship LM0?015-03 (R.L.S.) from the National Library of Medicine is gratefully acknowledged. We also wish to thank Dr. Ted Sakai for discussions. The NMR experiments were performed on a Bruker WH-400 NMR spectrometer at the NMR Core Facility of the Comprehensive Cancer Center which is operated under a grant from the U. S. Public Health Service (CA-13148) (J. R. Durant).
PY - 1982/9
Y1 - 1982/9
N2 - 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.
AB - 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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U2 - 10.1016/0003-9861(82)90525-2
DO - 10.1016/0003-9861(82)90525-2
M3 - Article
C2 - 6753747
AN - SCOPUS:0020186950
SN - 0003-9861
VL - 217
SP - 468
EP - 472
JO - Archives of Biochemistry and Biophysics
JF - Archives of Biochemistry and Biophysics
IS - 2
ER -