Abstract

The overall research plan is to describe the protein and DNA of the filamentous bacteriophages. NMR spectroscopy of the viral nucleoprotein complexes and the coat protein in reconstituted phospholipid bilayers enables this description of the protein and DNA, and their interactions, to be at the biophysical level of detail. The structure of the coat protein in the virus is being determined by the solid state NMR experiments on virus samples oriented in the magnetic field of the spectrometer. The method for structure determination takes advantage of the spectral simplifications that accompany macroscopic uniaxial orientation of a polymeric samples parallel to the applied magnetic field. The angular dependent of the nuclear spin interactions is then used to determine the orientation of individual sites. The motions of the DNA and protein in the virus and of the protein in the virus and of the protein in lipid bilayers are being characterized. This is done in solid state NMR by explicitly separating geometrical and dynamical factors in the analysis of resonance lineshapes and relaxation parameters.

  Funding Agency

Agency
National Institute of Health (NIH)
Institute
National Institute of General Medical Sciences (NIGMS)
Type
Research Project (R01)
Project #
5R01GM024266-09
Application #
3272156
Study Section
Biophysics and Biophysical Chemistry B Study Section (BBCB)
Project Start
1977-08-01
Project End
1988-07-31
Budget Start
1985-08-01
Budget End
1986-07-31
Support Year
9
Fiscal Year
1985
Total Cost
Indirect Cost

  Institution

Name
University of Pennsylvania
Department
Type
Schools of Arts and Sciences
DUNS #
042250712
City
Philadelphia
State
PA
Country
United States
Zip Code
19104

  Publications

Rosay, M; Zeri, A C; Astrof, N S et al. (2001) Sensitivity-enhanced NMR of biological solids: dynamic nuclear polarization of Y21M fd bacteriophage and purple membrane. J Am Chem Soc 123:1010-1
Ramamoorthy, A; Opella, S J (1995) Two-dimensional chemical shift/heteronuclear dipolar coupling spectra obtained with polarization inversion spin exchange at the magic angle and magic-angle sample spinning (PISEMAMAS). Solid State Nucl Magn Reson 4:387-92
Ramamoorthy, A; Wu, C H; Opella, S J (1995) Three-dimensional solid-state NMR experiment that correlates the chemical shift and dipolar coupling frequencies of two heteronuclei. J Magn Reson B 107:88-90
Opella, S J (1994) Solid-state NMR structural studies of proteins. Annu Rev Phys Chem 45:659-83
Opella, S J; Kim, Y; McDonnell, P (1994) Experimental nuclear magnetic resonance studies of membrane proteins. Methods Enzymol 239:536-60
Bechinger, B; Zasloff, M; Opella, S J (1993) Structure and orientation of the antibiotic peptide magainin in membranes by solid-state nuclear magnetic resonance spectroscopy. Protein Sci 2:2077-84
McDonnell, P A; Shon, K; Kim, Y et al. (1993) fd coat protein structure in membrane environments. J Mol Biol 233:447-63
Bechinger, B; Zasloff, M; Opella, S J (1992) Structure and interactions of magainin antibiotic peptides in lipid bilayers: a solid-state nuclear magnetic resonance investigation. Biophys J 62:12-4
Bechinger, B; Kim, Y; Chirlian, L E et al. (1991) Orientations of amphipathic helical peptides in membrane bilayers determined by solid-state NMR spectroscopy. J Biomol NMR 1:167-73
Opella, S J; Stewart, P L (1989) Solid-state nuclear magnetic resonance structural studies of proteins. Methods Enzymol 176:242-75

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