CONFORMATION OF SURFACE-EXPOSED N-TERMINUS PART OF BACTERIORHODOPSIN STUDIED BY TRANSFERRED NOE TECHNIQUE

Interaction of the monoclonal antibody A5 raised against native bacter iorhodopsin (BR) with the synthetic peptide pGlu(1)-Ala-Gln-Ile-Thr-Gl y-Arg(7)-NH2, corresponding to the amino acid sequence 1-7 was studied by transferred nuclear Overhauser effect (TRNOE) spectroscopy, The de naturing reagents and the specially designed pulse sequences which eli minate broad signals from the TRNOE spectra were used to favour evalua tion of the TRNOE peaks, On the basis of the data obtained, the confor mation of peptide bound with A5 was calculated, A model of the mutual arrangement of bacteriorhodopsin N-terminus and the first transmembran e alpha-helical segment 8-32 was proposed.