Circular Dichroism Studies on Turnip Rosette Virus

Summary Circular dichroism studies show that the RNA of turnip rosette virus (TRosV), both within the particles and free in solution, has considerable base pairing. The protein of TRosV is characterized by a relatively high proportion of β-structure and low proportion of α-helix. Swelling of the virus particles by raising the pH and removing divalent cations causes slight changes in the conformation of the RNA and some changes in the protein conformation.

[1]  R. Hull.  The stabilization of the particles of turnip rosette virus. III. Divalent cations. , 1978, Virology.

[2]  A. Tamburro,et al.  Circular dichroism studies of chicory yellow mottle virus , 1977 .

[3]  R. Hull,et al.  The in vitro crystalline formations of turnip rosette virus. I. Electron microscopy of two- and three-dimensional arrays. , 1977, Virology.

[4]  J. Brahms,et al.  Identification of β,β-turns and unordered conformations in polypeptide chains by vacuum ultraviolet circular dichroism , 1977 .

[5]  R. Hull.  The Grouping of Small Spherical Plant Viruses with Single RNA Components , 1977 .

[6]  R. Hull.  The stabilization of the particles of turnip rosette virus and of other members of the southern bean mosaic virus group. , 1977, Virology.

[7]  R. Hammonds.  Least-squares analysis of circular dichroic spectra of proteins. , 1977, European journal of biochemistry.

[8]  K. A. Hartman,et al.  Studies of virus structure by laser-Raman spectroscopy. 3. Turnip yellow mosaic virus , 1976 .

[9]  K. A. Hartman,et al.  Studies of virus structure by laser-Raman spectroscopy. II. MS2 phage, MS2 capsids and MS2 RNA in aqueous solutions. , 1976, Journal of molecular biology.

[10]  C. Baker,et al.  On the analysis of circular dichroic spectra of proteins. , 1976, Biochemistry.

[11]  G. Thomas,et al.  Structure of coat proteins in Pf1 and fd virions by laser raman spectroscopy. , 1975, Science.

[12]  R. M. Goodman,et al.  Circular dichroism and fluorescence studies on potato virus X and its structural components. , 1975, Biochimica et biophysica acta.

[13]  D. Marvin,et al.  Structure and assembly of filamentous bacterial viruses , 1975, Nature.

[14]  Y H Chen,et al.  Determination of the helix and beta form of proteins in aqueous solution by circular dichroism. , 1974, Biochemistry.

[15]  R. Jaenicke,et al.  Conformational changes and proton uptake in the reversible aggregation of tobacco-mosaic-virus protein. , 1974, European journal of biochemistry.

[16]  J. Flanegan,et al.  Noncovalent interactions in viruses: characterization of their role in the pH and thermally induced conformational changes in bromegrass mosaic virus. , 1973, Virology.

[17]  P. Boulanger,et al.  Conformational study of adenovirus type 2 hexon and fiber antigens. , 1972, Biochemical and biophysical research communications.

[18]  D. Gordon.  LIGHT SCATTERING BY OPTICALLY ACTIVE PARTICLES , 1972 .

[19]  W. Gratzer,et al.  Evaluation of RNA conformation from circular dichroism and optical rotatory dispersion data , 1971, Biopolymers.

[20]  W. Gratzer,et al.  Secondary structure and interaction of RNA and protein in a bacteriophage. , 1971, Biochimica et biophysica acta.

[21]  G. Fasman,et al.  Computed circular dichroism spectra for the evaluation of protein conformation. , 1969, Biochemistry.

[22]  D. Schubert.  Conformational changes during reversible depolymerization of the protein coat from bacteriophage. , 1969, Biochimica et biophysica acta.

[23]  J. Brahms,et al.  Conformational stability of dinucleotides in solution. , 1967, Journal of molecular biology.

[24]  D. Schlessinger.  Hypochromicity in ribosomes from Escherichia coli , 1960 .

[25]  D. Gordon.  Mie scattering by optically active particles. , 1972, Biochemistry.

[26]  T. Tikchonenko.  Conformation of viral nucleic acids in situ. , 1969, Advances in virus research.