Single-strand deoxyribonucleic acid binding protein from rat liver changes the helical structure of deoxyribonucleic acid
- 9 June 1981
- journal article
- research article
- Published by American Chemical Society (ACS) in Biochemistry
- Vol. 20 (12) , 3598-3603
- https://doi.org/10.1021/bi00515a045
Abstract
Note: In lieu of an abstract, this is the article's first page.This publication has 10 references indexed in Scilit:
- Interaction between the adenovirus DNA-binding protein and double-stranded DNAJournal of Molecular Biology, 1979
- Torsional stress and local denaturation in supercoiled DNA.Proceedings of the National Academy of Sciences, 1979
- Nicking-closing enzyme assembles nucleosome-like structures in vitro.Proceedings of the National Academy of Sciences, 1979
- E. coli DNA binding protein HU forms nucleosome-like structure with circular double-stranded DNACell, 1979
- An Escherichia coli mutant defective in single-strand binding protein is defective in DNA replication.Proceedings of the National Academy of Sciences, 1979
- A deoxyribonucleic acid unwinding protein isolated from regenerating rat liver. Physical and functional properties.Journal of Biological Chemistry, 1978
- Supercoiling in closed circular DNA: dependence upon ion type and concentrationBiochemistry, 1978
- DNA "melting" proteins. IV. Fluorescence measurements of binding parameters for bacteriophage T4 gene 32-protein to mono-, oligo-, and polynucleotides.Journal of Biological Chemistry, 1976
- Linking numbers and nucleosomes.Proceedings of the National Academy of Sciences, 1976
- A new preparation method for dark-field electron microscopy of biomacromoleculesJournal of Ultrastructure Research, 1971