ASSIGNMENT OF H-1, N-15, AND BACKBONE C-13 RESONANCES IN DETERGENT-SOLUBILIZED M13 COAT PROTEIN VIA MULTINUCLEAR MULTIDIMENSIONAL NMR - A MODEL FOR THE COAT PROTEIN MONOMER

The major coat protein (gVIIIp) of bacteriophage M13 complexed with SD S detergent micelles was used as a model system to study the lipid-bou nd conformation of the protein. Conditions were found that allowed the recording of good quality of NMR spectra. By making extensive use of three-dimensional heteronuclear (C-13, N-15) NMR, we obtained a comple te set of resonance assignments for (HN)-H-1, H-1alpha, H-1beta, C-13a lpha, CO, and N-15 and partially assigned the rest of the H-1 spectrum . Analysis of NOE and chemical shift data reveals that gVIIIp is compo sed of two alpha-helical domains, one ranging from Pro-6 to Glu20 and the other ranging from Tyr-24 all the way to the C-terminus Ser-50. In contrast to the results reported by Henry and Sykes [Henry, G. D., & Sykes, B. D. (1992) Biochemistry 31, 5285-5297], at a high SDS to prot ein ratio the protein appears to be monomeric.