Structure and dynamics of the Pf1 filamentous bacteriophage coat protein in micelles.
The major coat protein of filamentous bacteriophage adopts its membrane-bound conformation in detergent micelles. High-resolution 1H and 15N NMR experiments are used to characterize the structure and dynamics of residues 30-40 in the hydrophobic midsection of Pf1 coat protein in sodium dodecyl sulfate micelles. Uniform and specific-site 15N labels enable the immobile backbone sites to be identified by their 1H/15N heteronuclear nuclear Overhauser effect and allow the assignment of 1H and 15N resonances. About one-third of the amide N-H protons in the protein undergo very slow exchange with solvent deuterons, which is indicative of sites in highly structured environments. The combination of results from 1H/15N heteronuclear correlation, 1H homonuclear correlation, and 1H homonuclear Overhauser effect experiments assigns the resonances to specific residues and demonstrates that residues 30-40 of the coat protein have a helical secondary structure.
D000577:Amides; D002213:Capsid / Q000648:ultrastructure; D003090:Coliphages / Q000648:ultrastructure*; D006860:Hydrogen Bonding; D009682:Magnetic Resonance Spectroscopy; D008565:Membrane Proteins; D008823:Micelles; D011487:Protein Conformation; D013057:Spectrum Analysis; D014443:Tyrosine
D000577:Amides; D008565:Membrane Proteins; D008823:Micelles; D014443:Tyrosine