Hydrodynamic studies of a DNA‐protein complex

FEBS Letters

van Grondelle, R.¹  Blok, Joh.¹  Kuil, M.E.¹  Scheerhagen, M.A.¹ 

[1] Department of Biophysics, Free University, De Boelelaan 1081, 1081 HV Amsterdam, The Netherlands

关键词: DNA-protein complex Helix-destabilizing protein Bacteriophage T4 Quasi-elastic light scattering Hydrodynamic dimensions;   

DOI  :  10.1016/0014-5793(85)80610-4

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown