Structure and dynamics of the membrane-bound form of the filamentous bacteriophage coat proteins by NMR spectroscopy
The structure and dynamics of the Pf1 and fd bacteriophage coat proteins in detergent micelles are characterized in solution by nuclear magnetic resonance spectroscopy. The coat proteins are found to exist within the bacterial inner cell membrane during viral infection and assembly. The coat proteins serve as a model system to investigate integral membrane proteins as well as the viral infection and assembly processes. The coat protein is insoluble in aqueous or organic solvents and can only be effectively solubilized in the presence of detergents that form micelles or phospholipids that form vesicles. The effective molecular weight of the detergent-micelle complex is ca. 30K daltons. Sequential assignment strategies were ineffective due to short T/sub 2s/ and severe resonance degeneracy. The backbone resonance assignments were completed by the combination of several homo- and heteronuclear correlation techniques with biosynthetic /sup 15/N labelling. 2D NOE experiments were used to locate and characterize the secondary structure of the membrane bound form of the proteins showing them to be largely helical with the hydrophobic core existing in a very stable helix.
- Research Organization:
- Pennsylvania Univ., Philadelphia (USA)
- OSTI ID:
- 6945404
- Country of Publication:
- United States
- Language:
- English
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Related Subjects
59 BASIC BIOLOGICAL SCIENCES
BACTERIOPHAGES
BIOLOGICAL MODELS
CELL CONSTITUENTS
CELL MEMBRANES
CELL WALL
ISOTOPES
LIGHT NUCLEI
MEMBRANE PROTEINS
MEMBRANES
MICROORGANISMS
MOLECULAR STRUCTURE
NITROGEN 15
NITROGEN ISOTOPES
NMR SPECTRA
NUCLEI
ODD-EVEN NUCLEI
ORGANIC COMPOUNDS
PARASITES
PROTEINS
SPECTRA
STABLE ISOTOPES
VIRUSES