Two-dimensional1H-nmr study of synthetic peptides containing the main immunogenic region of theTorpedo acetylcholine receptor
| Autor: | Michel Marraud, Anna Kokla, E. Bairaktari, I. Hadjidakis, C. Sakarellos, Socrates J. Tzartos, Manh-Thong Cung |
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| Rok vydání: | 1989 |
| Předmět: |
Magnetic Resonance Spectroscopy
Proton Protein Conformation Stereochemistry Molecular Sequence Data Biophysics Receptors Cholinergic/immunology Biochemistry law.invention Biomaterials Epitopes chemistry.chemical_compound law Amide Receptors Cholinergic Amino Acid Sequence Spectroscopy Magnetic Resonance Spectroscopy/methods Acetylcholine receptor Organic Chemistry General Medicine Oligopeptides/chemical synthesis chemistry Intramolecular force Proton NMR Oligopeptides Two-dimensional nuclear magnetic resonance spectroscopy Torpedo Hydrogen |
| Zdroj: | Biopolymers. 28:465-478 |
| ISSN: | 1097-0282 0006-3525 |
| DOI: | 10.1002/bip.360280141 |
| Popis: | A comparative 1H-NMR spectral study of a synthetic decapeptide containing the main immunogenic region of the Torpedo acetylcholine receptor (AChR; WNPADYGGIK, representing the alpha 67-76 fragment of Torpedo AChR) with four analogous peptides (WNP3-D5YGGIK, WNPAA5YGGIK, WNPADYGGA9K, and WNPD4DYGGV9K) has been carried out in dimethyl sulfoxide. One- and two-dimensional nmr experiments [correlated spectroscopy (COSY), relayed COSY, and phase-sensitive nuclear Overhauser enhancement spectroscopy (NOESY)] were performed to obtain complete assignments of the proton resonances. The presence of strong and multiple short- and long-range NOEs, and especially a strong long-range NOE between the two Asn2-C alpha H and Gly7-C alpha H protons, argues in favor of a rigid folded structure in all five cases. Temperature dependence measurements indicate the existence of three intramolecular interactions involving the Asp3, Gly8, and Lys10 amide protons. Biopolymers |
| Databáze: | OpenAIRE |
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