Two-dimensional 1H-nmr study of synthetic peptides containing the main immunogenic region of the Torpedo acetylcholine receptor
β Scribed by M. T. Cung; M. Marraud; I. Hadjidakis; E. Bairaktari; C. Sakarellos; A. Kokla; S. Tzartos
- Publisher
- Wiley (John Wiley & Sons)
- Year
- 1989
- Tongue
- English
- Weight
- 679 KB
- Volume
- 28
- Category
- Article
- ISSN
- 0006-3525
No coin nor oath required. For personal study only.
β¦ Synopsis
synopms
A comparative 'H-NMR spectral study of a synthetic decapeptide containing the main immunogenic region of the Torpedo acetylcholine receptor (AChR; WNPADYGGIK, representing the a67-76 fragment of Torpedo AChR) with four analogous peptides (WNP3-D5YGGIK, WNPAA5YGGIK, WNPADYGGA'K, and WNPD4DYGGV'K) has been carried out in dimethyl sulfoxide.
One-
and two-dimenional 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 shortand long-range NOES, and especially a strong long-range NOE between the two Asn'-CaH and Gly7-CaH 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 As#, Gly', and Lys" amide protons.
π SIMILAR VOLUMES
## Binding of autoantibodies to the acetylcholine receptor (AChR) plays a major role in the autoimmune disease Myasthenia gravis (MG). In this paper, we propose a structure model of a putative immunocomplex that gives rise to the reduction of functional AChR molecules during the course of MG. The mo
Two-dimensional NMR experiments [correlated spectroscopy (COSY) and two-dimensional transferred nuclear Overhauser enhancement spectroscopy (TR-NOESY) ] have been applied to study the interactions of a monoclonal antibody (mAb) directed to the main immunogenic region (MIR) of the acetylcholine recep
## Monoclonal antibodies against the main immunogenic region (MIR) of the muscle acetylcholine receptor (AChR) are capable of inducing experimental myasthenia gravis ( M G ) in animals. The epitope of these antibodies has been localized between residues 67 and 76 of the AChR a-subunit. The conformat