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Solution Conformation of Peptides Through 1H Nuclear Magnetic Double Resonance Measurement of Amide Hydrogen Exchange Rates: Study of the Active Pentapeptide Fragment of Thymopoietin

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Abstract:

The amide hydrogen exchange rates of peptides (and other biomolecules) can be related to their secondary and tertiary structures. The exchange rates in the range ∼0.1 to ∼100 s−1 can be conveniently measured in H2O by a double resonance technique involving a combination of two separate 1H NMR experiments: (1) the transfer of solvent saturation and (2) the selective saturation recovery of the labile hydrogen. When a peptide exists in a dynamic equilibrium among several conformations, the interpretation of the above two experiments in terms of intrinsic exchange rates is not straightforward in general. The effect of a multistate conformational averaging is considered in the interpretation of the above two experiments, and analytical expressions have been presented for a few limiting cases of conformational and chemical equilibria. The amide hydrogen exchange rates of the pentapeptide Arg-Lys-Asp-Val-Tyr, the active fragment of the thymic hormone thymopoietin, have been measured in H2O through the transfer of solvent saturation and saturation recovery experiments. The results suggest that this fragment exists in a highly motile dynamic equilibrium among several conformations. In some of these, the Val4 NH hydrogen is shielded significantly from the solvent.

Keywords: Nuclear magnetic double resonance spectroscopy

Document Type: Research Article

DOI: http://dx.doi.org/10.1366/0003702804731456

Affiliations: 1: Comprehensive Cancer Center, Departments of Biochemistry and Physics, University of Alabama in Birmingham, Birmingham, Alabama 35294 2: Comprehensive Cancer Center, Department of Physics, University of Alabama in Birmingham, Birmingham, Alabama 35294 3: Ortho Pharmaceutical Corporation, Raritan, New Jersey 08864

Publication date: July 1, 1980

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