A robust method is proposed for identifying the putative bioactive conformation of linear peptide analogues of myelin basic protein, which induce the EAE (experimental autoimmune encephalomyelitis) instructive model for the investigation of multiple sclerosis. Their conformational and binding properties were compared with the properties of EAE antagonist. Specific conformational properties of EAE agonist and antagonist were elucidated, which determine differences in their interactions with T-cell receptor.
COBISS.SI-ID: 3843610
The conformational properties of dipeptides in water solution were examined with a combination of vibrational and NMR methods. Our results indicate that currently the best theoretical methods for proteins can not accurately predict even the backbone structure of dipetides. A probable explanation is incorrect theoretical description of non-bonded interactions in proteins or peptides. The results are important for the development of new force fields for studies of conformation, dynamics and interactions of proteins, including ligand-protein interactions.
COBISS.SI-ID: 3877146