Conformational studies of N-Tyr-MIF-1 in aqueous solution by 1H nuclear magnetic resonance spectroscopy
| Autor: | Roberta L. Moldow, H.N. Halladay, M. Petersheim, A.J. Fischman, Abba J. Kastin |
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| Rok vydání: | 2009 |
| Předmět: |
education.field_of_study
Magnetic Resonance Spectroscopy Tetrapeptide Protein Conformation Stereochemistry Spectrum Analysis Chemical shift Molecular Sequence Data Population Temperature Water Stereoisomerism Nuclear magnetic resonance spectroscopy Biochemistry MSH Release-Inhibiting Hormone Pyrrolidine Solutions chemistry.chemical_compound Models Chemical chemistry Amino Acid Sequence education Conformational isomerism Two-dimensional nuclear magnetic resonance spectroscopy Cis–trans isomerism |
| Zdroj: | International Journal of Peptide and Protein Research. 40:41-48 |
| ISSN: | 0367-8377 |
| DOI: | 10.1111/j.1399-3011.1992.tb00102.x |
| Popis: | N-Tyr-MIF-1 (Tyr-Pro-Leu-Gly-NH2) is an endogenous brain peptide with multiple effects on animal behavior. However, there have been no studies on the conformation of this tetrapeptide. In this report, we studied the conformation of N-Tyr-MIF-1 in aqueous solution by conventional one-dimensional and two-dimensional (COSY and NOESY) 1H nuclear magnetic resonance spectroscopy at 300 MHz. A complete set of assignments for the resolved resonances and approximate assignments for the overlapping resonances were made. The results demonstrate that N-Tyr-MIF-1 is in slow exchange between two conformers, most likely determined by the cis and trans states of the proline residue. The minor conformation represents 30 +/- 3% of the population over the temperature range from 3 degrees to 73 degrees. In the major conformation, the tyrosine aromatic ring appears to be close enough to interact directly with the proline pyrrolidine ring, as indicated by a strong temperature dependence of the proline C beta H, C delta H and C delta H' chemical shifts. In contrast, this interaction of the tyrosine and proline rings is not present in the minor conformation. |
| Databáze: | OpenAIRE |
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