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 /sup 1/H and /sup 15/N 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 /sup 15/N labels enable the immobile backbone sites to be identified by their /sup 1/H//sup 15/N heteronuclear nuclear Overhauser effect and allow the assignment of /sup 1/H and /sup 15/N 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 /sup 1/H//sup 15/N heteronuclear correlation, /sup 1/H homonuclear correlation, and /sup 1/H 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.
- Research Organization:
- Univ. of Pennsylvania, Philadelphia
- OSTI ID:
- 6219865
- Journal Information:
- Biochemistry; (United States), Journal Name: Biochemistry; (United States) Vol. 26:5; ISSN BICHA
- Country of Publication:
- United States
- Language:
- English
Similar Records
Structure and dynamics of the membrane-bound form of the filamentous bacteriophage coat proteins by NMR spectroscopy
Pf1 bacteriophage hydration by magic angle spinning solid-state NMR
Related Subjects
62 RADIOLOGY AND NUCLEAR MEDICINE
BACTERIOPHAGES
BARYONS
DICHROISM
ELEMENTARY PARTICLES
FERMIONS
HADRONS
ISOTOPES
LIGHT NUCLEI
MAGNETIC RESONANCE
MICROORGANISMS
MOLECULAR STRUCTURE
NITROGEN 15
NITROGEN ISOTOPES
NUCLEAR MAGNETIC RESONANCE
NUCLEI
NUCLEONS
ODD-EVEN NUCLEI
ORGANIC COMPOUNDS
OVERHAUSER EFFECT
PARASITES
PROTEINS
PROTONS
RESONANCE
STABLE ISOTOPES
VIRUSES