Our studies on polyoma virus, membrane gap junctions, tobacco mosaic virus and filamentous bacteriophage are focused on correlating their structures with the dynamic processes in their formation, interactions and stability. Coordinated X-ray diffraction, electron microscopy, spectroscopy and physico-chemical methods are being applied in these studies. Polyoma virus structure is being analyzed by X-ray crystallography of the intact virion and empty protein capsid to determine details of the structure and packing of the 72 pentameric capsomeres that build this icosahedrally symmetric structure. Low-irradiation electron micrographs of tubular polymorphic polyoma capsomere assemblies are being processed to characterize the variable bonding interactions. Model building will be used to correlate structural information about the switching in bonding specificity of polyoma capsomeres obtained by X-ray diffraction and electron microscopy. Improved methods of purifying and orienting gap junction specimens are making possible systematic X-ray diffraction and electron microscope studies of controlled structual and chemical modifications related to the mechanisms that regulate intercellular communication. The Beta-sheet conformation of the connexon protein is being characterized from the high angle X-ray diffraction. Chemical modification of tyrosine residues in tobacco mosaic virus and filamentous bacteriophage is being studied by spectroscopic titration to relate electrostatic interaction with the structure. Interparticle interactions in liquid and colloid crystalline phases of rod-shaped viruses oriented in magnetic field are being studied by light and X-ray scattering. A TV area detector will be used for diffraction measurements on virus and membrane specimens that could not be carried out by photographic recording.

Agency
National Institute of Health (NIH)
Institute
National Cancer Institute (NCI)
Type
Research Project (R01)
Project #
2R01CA015468-12
Application #
3164178
Study Section
Biophysics and Biophysical Chemistry B Study Section (BBCB)
Project Start
1975-01-01
Project End
1989-12-31
Budget Start
1985-01-01
Budget End
1985-12-31
Support Year
12
Fiscal Year
1985
Total Cost
Indirect Cost
Name
Brandeis University
Department
Type
Organized Research Units
DUNS #
616845814
City
Waltham
State
MA
Country
United States
Zip Code
Li, Jade; Fricks, Carl; Rayment, Ivan et al. (2017) Reversible swelling of SBMV is associated with reversible disordering. J Struct Biol 200:314-324
Sosinsky, G E (1992) Image analysis of gap junction structures. Electron Microsc Rev 5:59-76
Sosinsky, G E; Baker, T S; Caspar, D L et al. (1990) Correlation analysis of gap junction lattice images. Biophys J 58:1213-26
Oldenbourg, R; Ruiz, T (1989) Birefringence of macromolecules. Wiener's theory revisited, with applications to DNA and tobacco mosaic virus. Biophys J 56:195-205
Salunke, D M; Caspar, D L; Garcea, R L (1989) Polymorphism in the assembly of polyomavirus capsid protein VP1. Biophys J 56:887-900
Sosinsky, G E; Jesior, J C; Caspar, D L et al. (1988) Gap junction structures. VIII. Membrane cross-sections. Biophys J 53:709-22
Namba, K; Caspar, D L; Stubbs, G (1988) Enhancement and simplification of macromolecular images. Biophys J 53:469-75
Salunke, D M; Caspar, D L; Garcea, R L (1986) Self-assembly of purified polyomavirus capsid protein VP1. Cell 46:895-904
Raghavendra, K; Salunke, D M; Caspar, D L et al. (1986) Disk aggregates of tobacco mosaic virus protein in solution: electron microscopy observations. Biochemistry 25:6276-9
Winkelmann, D A; Mekeel, H; Rayment, I (1985) Packing analysis of crystalline myosin subfragment-1. Implications for the size and shape of the myosin head. J Mol Biol 181:487-501

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