Structure and dynamics of the fd coat protein
The structure and dynamics of the coat protein of the filamentous bacteriophage, fd, are studied using a combination of novel solid-state NMR techniques. The fd coat protein exists in two conformational states during the viral lifecycle, as the major structural element of the intact virus particle and as an integral membrane protein. The comparison of these two forms of the coat protein leads to insights into the assembly process of the bacteriophage. The dynamic studies of the coat protein entail the use of lineshape analysis of the /sup 15/N chemical shift anisotropy for the amide backbone site. This interaction can distinguish large amplitude motions of an amide site from a rigid amide site on the timescale of 10/sup 3/ Hz. Biosynthetic labelling with specific /sup 15/N amino acids in the coat protein backbone, allows the interpretation of dynamics at atomic resolution within the entire coat protein backbone. The structural studies of the coat protein in the intact virus particle use of the angular information derived from orientation dependent spin interactions. The dynamic studies of the fd coat protein have found the four N-terminal residues to be mobile in the two environments. The remaining stretch of 46 residues is held to a rigid conformation as the structural protein in the intact virus particle. In the membrane environment, the central hydrophobic core of the coat protein is held rigid within the membrane bilayer with the final five or six C-terminal residues mobile. The structure of the immobile portion of the coat protein in the intact virus was determined to be an extended ..cap alpha..-helix with a bend around the central VAL-30-VAL-31 residues of the coat protein.
- Research Organization:
- Pennsylvania Univ., Philadelphia (USA)
- OSTI ID:
- 6701137
- Resource Relation:
- Other Information: Thesis (Ph. D.)
- Country of Publication:
- United States
- Language:
- English
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Related Subjects
PROTEINS
CONFORMATIONAL CHANGES
NUCLEAR MAGNETIC RESONANCE
STRUCTURAL CHEMICAL ANALYSIS
ANISOTROPY
BACTERIOPHAGES
CHEMICAL SHIFT
NITROGEN 15
ISOTOPES
LIGHT NUCLEI
MAGNETIC RESONANCE
MICROORGANISMS
NITROGEN ISOTOPES
NUCLEI
ODD-EVEN NUCLEI
ORGANIC COMPOUNDS
PARASITES
RESONANCE
STABLE ISOTOPES
VIRUSES
550601* - Medicine- Unsealed Radionuclides in Diagnostics