A mutation in E. coli SSB protein (W54S) alters intra-tetramer negative cooperativity and inter-tetramer positive cooperativity for single-stranded DNA binding (Q73289701)

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scientific article published on 01 February 1997

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English	A mutation in E. coli SSB protein (W54S) alters intra-tetramer negative cooperativity and inter-tetramer positive cooperativity for single-stranded DNA binding	scientific article published on 01 February 1997

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scholarly article

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2 November 2019

A mutation in E. coli SSB protein (W54S) alters intra-tetramer negative cooperativity and inter-tetramer positive cooperativity for single-stranded DNA binding (English)

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2 November 2019

Escherichia coli

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M E Ferrari

1

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2 November 2019

J Fang

2

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2 November 2019

T M Lohman

3

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2 November 2019

publication date

1 February 1997

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2 November 2019

Biophysical Chemistry

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2 November 2019

64

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2 November 2019

1-3

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2 November 2019

235-251

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2 November 2019

Single-stranded DNA binding proteins required for DNA replication

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Escherichia coli single-stranded DNA-binding protein: multiple DNA-binding modes and cooperativities

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Equilibrium binding of Escherichia coli single-strand binding protein to single-stranded nucleic acids in the (SSB)65 binding mode. Cation and anion effects and polynucleotide specificity.

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Fluorescence and chemical studies on the interaction of Escherichia coli DNA-binding protein with single-stranded DNA

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Negative co-operativity in Escherichia coli single strand binding protein-oligonucleotide interactions. I. Evidence and a quantitative model

1 reference

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Negative co-operativity in Escherichia coli single strand binding protein-oligonucleotide interactions. II. Salt, temperature and oligonucleotide length effects

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Escherichia coli single-strand binding protein forms multiple, distinct complexes with single-stranded DNA

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Negative cooperativity within individual tetramers of Escherichia coli single strand binding protein is responsible for the transition between the (SSB)35 and (SSB)56 DNA binding modes

1 reference

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Effects of base composition on the negative cooperativity and binding mode transitions of Escherichia coli SSB-single-stranded DNA complexes

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Monomers of the Escherichia coli SSB-1 mutant protein bind single-stranded DNA.

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Salt-dependent changes in the DNA binding co-operativity of Escherichia coli single strand binding protein.

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Limited co-operativity in protein-nucleic acid interactions. A thermodynamic model for the interactions of Escherichia coli single strand binding protein with single-stranded nucleic acids in the "beaded", (SSB)65 mode

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Co-operative binding of Escherichia coli SSB tetramers to single-stranded DNA in the (SSB)35 binding mode

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T4 Bacteriophage Gene 32: A Structural Protein in the Replication and Recombination of DNA

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Kinetics and mechanism of dissociation of cooperatively bound T4 gene 32 protein-single-stranded nucleic acid complexes. 1. Irreversible dissociation induced by sodium chloride concentration jumps

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Viability and preliminary in vivo characterization of site-directed mutants of Escherichia coli single-stranded DNA-binding protein

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Large-scale overproduction and rapid purification of the Escherichia coli ssb gene product. Expression of the ssb gene under lambda PL control.

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Apparent heat capacity change accompanying a nonspecific protein-DNA interaction. Escherichia coli SSB tetramer binding to oligodeoxyadenylates

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A general method of analysis of ligand-macromolecule equilibria using a spectroscopic signal from the ligand to monitor binding. Application to Escherichia coli single-strand binding protein-nucleic acid interactions.

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Identifiers

10.1016/S0301-4622(96)02223-5

1 reference

Europe PubMed Central

PubMed publication ID

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2 November 2019

PubMed publication ID

1 reference

Europe PubMed Central

PubMed publication ID

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:9127948%20AND%20SRC:MED&resulttype=core&format=json

2 November 2019

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