Hydrodynamic studies of a DNA-protein complex
Author:
Publisher
Wiley
Subject
Cell Biology,Genetics,Molecular Biology,Biochemistry,Structural Biology,Biophysics
Link
http://onlinelibrary.wiley.com/wol1/doi/10.1016/0014-5793(85)80610-4/fullpdf
Reference20 articles.
1. Interactions of bacteriophage T4-coded gene 32 protein with nucleic acids
2. Fluorescence study of the association between gene 32 protein of bacteriophage T4 and . Evidence for energy transfer
3. Chemical modifications of functional residues of fd gene 5 DNA-binding protein
Cited by 14 articles. 订阅此论文施引文献 订阅此论文施引文献，注册后可以免费订阅5篇论文的施引文献，订阅后可以查看论文全部施引文献
1. C-terminal Domain of T4 gene 32 Protein Enables Rapid Filament Reorganization and Dissociation;Journal of Molecular Biology;2024-05
2. Dynamic structure of T4 gene 32 protein filaments facilitates rapid noncooperative protein dissociation;Nucleic Acids Research;2023-07-14
3. Study of the binding of single-stranded DNA-binding protein to DNA and poly(rA) using electric field induced birefringence and circular dichroism spectroscopy;Biochemistry;1990-09-04
4. Structure calculations for single-stranded DNA complexed with the single-stranded DNA binding protein GP32 of bacteriophage T4: a remarkable DNA structure;Biochemistry;1990-06-12
5. A Refined Calculation of the Solution Dimensions of the Complex Between Gene 32 Protein and Single Stranded DNA Based on Estimates of the Bending Persistence Length;Journal of Biomolecular Structure and Dynamics;1990-02
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