A capillary electrophoresis mobility shift assay for protein—DNA binding affinities free in solution

Quantitative determination of dissociation constants for DNA-protein complexes will help clarify the molecular mechanisms of transcription, replication and DNA repair. A practical capillary electrophoresis mobility shift assay (CEMSA) for protein—DNA affinities free in solution is presented. The met...

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Bibliographic Details
Published in:Nucleic acids research 1998-09, Vol.26 (18), p.4304-4305
Main Authors: Foulds, Glenn J., Etzkorn, Felicia A.
Format: Article
Language:English
Subjects:
Binding Sites
DNA - chemistry
DNA - metabolism
DNA-Binding Proteins - metabolism
Electrophoresis, Capillary - methods
Fungal Proteins - chemistry
Fungal Proteins - isolation & purification
Fungal Proteins - metabolism
Kinetics
Oligodeoxyribonucleotides - chemistry
Oligodeoxyribonucleotides - isolation & purification
Oligodeoxyribonucleotides - metabolism
Peptide Fragments - chemistry
Peptide Fragments - metabolism
Protein Kinases - chemistry
Protein Kinases - isolation & purification
Protein Kinases - metabolism
Reproducibility of Results
Saccharomyces cerevisiae - metabolism
Saccharomyces cerevisiae Proteins
Solutions
Transcription Factor AP-1 - chemistry
Transcription Factor AP-1 - metabolism
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Summary:Quantitative determination of dissociation constants for DNA-protein complexes will help clarify the molecular mechanisms of transcription, replication and DNA repair. A practical capillary electrophoresis mobility shift assay (CEMSA) for protein—DNA affinities free in solution is presented. The method is fast and simple, precise and general. The speed (
ISSN:0305-1048
1362-4962
1362-4962
DOI:10.1093/nar/26.18.4304