Hydrodynamic studies of a DNA‐protein complex

FEBS Letters

van Amerongen, H.¹  van Grondelle, R.¹  Blok, Joh.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;    Electric birefringence Axial increment determination;   

DOI  :  10.1016/0014-5793(85)80522-6

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Short DNA and RNA fragments complexed with the helix destabilizing protein of bacteriophage T4, GP32, have been studied in solution by electric birefringence and circular dichroism. The birefringence of the complexes is positive and the magnitude indicates that the DNA and RNA fragments become linear and rigid upon protein binding. The field free decay is biphasic. On the basis of a rigid rod approximation the slow relaxation time leads to a base-base distance along the helix axis in the complex from 4.3 to 5.6 Å, an elongation of at least 50% compared to single-stranded DNA.

【 授权许可】

Unknown