Role of tryptophan-14 in the interaction of dynorphin A(1-17) with micelles
| Autor: | Deborah A. Kallick, Michael R. Tessmer |
|---|---|
| Rok vydání: | 2009 |
| Předmět: |
Magnetic Resonance Spectroscopy
Protein Conformation Phosphorylcholine Molecular Sequence Data Molecular Conformation Analytical chemistry Context (language use) Dynorphin Dynorphins Biochemistry Micelle Fluorescence spectroscopy chemistry.chemical_compound Endocrinology Side chain Amino Acid Sequence Micelles Binding Sites Chemistry Tryptophan Dynorphin A Nuclear magnetic resonance spectroscopy Models Structural Spectrometry Fluorescence Critical micelle concentration Biophysics |
| Zdroj: | The Journal of Peptide Research. 49:427-431 |
| ISSN: | 1397-002X |
| Popis: | Fluorescence spectroscopy has been used to examine the interaction between the opioid peptide dynorphin A(1-17) (dynorphin) and dodecylphosphocholine (DPC) micelles. Fluorescence emission spectra as a function of added lipid indicate insertion of the Trp14 side chain into the hydrophobic portion of the micelle, supporting NMR results from this laboratory. A model of interaction with micelles consistent with the fluorescence results and earlier NMR results is proposed. The critical micelle concentration in the presence of peptide was also determined, and is discussed in the context of relevance to both NMR spectroscopy and peptide-lipid interactions. © Munksgaard 1997. |
| Databáze: | OpenAIRE |
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