Hydrodynamic studies of a DNA-protein complex: Dimensions of the complex of single-stranded 145 base DNA with gene 32 protein of phage T4 deduced from quasi-elastic light scattering

The translational diffusion coefficient of the saturated complex of single-stranded 145 base DNA and the helix-destabilizing protein of phage T4, GP32, can be measured at equilibrium by means of quasi-elastic light scattering. If the complex is considered as a rigid rod one can estimate its dimensio...

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Bibliographic Details
Published in:FEBS letters 1985-05, Vol.184 (2), p.221-225
Main Authors: Scheerhagen, M.A., Kuil, M.E., van Grondelle, R., Blok, Joh
Format: Article
Language:English
Subjects:
Biological and medical sciences
Deoxyribonucleoproteins
Diffusion
DNA
DNA, Single-Stranded
DNA-protein complex Helix-destabilizing protein Bacteriophage T4 Quasi-elastic light scattering Hydrodynamic dimensions
Fundamental and applied biological sciences. Psychology
Interactions. Associations
Intermolecular phenomena
Light
light scattering
Macromolecular Substances
Molecular biophysics
phage T4
proteins
Scattering, Radiation
T-Phages
Viral Proteins
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Description
Summary:The translational diffusion coefficient of the saturated complex of single-stranded 145 base DNA and the helix-destabilizing protein of phage T4, GP32, can be measured at equilibrium by means of quasi-elastic light scattering. If the complex is considered as a rigid rod one can estimate its dimensions by combining the translational diffusion coefficient with earlier data on rotational diffusion. It was found that the average base-base distance of the 145 base DNA in the complex is between 4.3 and 4.7 Å, while the diameter of the complex is between 44 and 68 Å. This suggests that the conformation of the complex must be such that a large amount of water is trapped.
ISSN:0014-5793
1873-3468
DOI:10.1016/0014-5793(85)80610-4