Protein structure by solid state nuclear magnetic resonance. Residues 40 to 45 of bacteriophage fd coat protein.
The three-dimensional structure of part of the coat protein in the filamentous bacteriophage fd is described by nuclear magnetic resonance (n.m.r.). Residues 40 to 45 are in a somewhat distorted alpha-helix. This n.m.r. approach for determining protein structure relies on the spectral manifestations of chemical shift and heteronuclear dipolar couplings in a symmetrical assembly of protein subunits oriented parallel to the applied magnetic field. The angles between individual peptide linkages and the filament axis of the virion constitute the basic source of structural information. These angles are directly related to x, y, z co-ordinates for describing the protein structure.
D000595:Amino Acid Sequence; D002213:Capsid; D055598:Chemical Phenomena; D002621:Chemistry; D003090:Coliphages / Q000032:analysis*; D009682:Magnetic Resonance Spectroscopy; D011487:Protein Conformation