We describe a simple two-dimensional electrophoresis procedure to identify the recognition sites of DNA-blnding proteins within large DNA molecules. Using this approach, we have mapped E.coll IHF (Integration Host Factor) binding sites within phage Lambda (48 kb) and phage Mu (39 kb) DNA. We are also able to visualize IHF binding sites in E.coll chromosomal DNA (4,700 kb). We present an extension of this technique using direct amplification by PCR of the Isolated restriction fragments, which should permit the cloning of a collection of recognition sequences for DNA binding proteins in complex genomes
Recognition of protein-DNA binding sites in genomic sequences is a crucial step for discovering biol...
Modern computational methods are revealing putative transcription-factor (TF) binding sites at an ex...
This chapter describes two-dimensional protein electrophoresis in phylogenetic studies. For molecula...
We applied phage display technology to DNA-protein interaction studies. A cDNA expression library di...
Abstract Background In a traditional electrophoresis mobility shift assay (EMSA) a 32P-labeled doubl...
We applied phage display technology to DNA-protein interaction studies. A cDNA expression library di...
Transcription factor-DNA interactions are some of the most important processes in biology because th...
We have used two-dimensional gel electrophoresis as a general „preparative” method to purify protein...
A novel strategy has been used to isolate a cDNA clone that encodes a DNA binding domain whose recog...
Phage display is a useful means of identifying and selecting proteins of interest that bind specific...
The aim of the work described in this thesis was to identify and characterise novel genes in the cla...
The integration host factor (IHF) of Escherichia coli is a small, sequence-specific DNA-binding prot...
The study of molecular recognition of DNA by natural and synthetic ligands has made enormous progres...
Transcription factors lie at the center of gene regulation, and their identification is crucial to t...
A method to detect DNA-binding sites on the surface of a protein structure is important for func-tio...
Recognition of protein-DNA binding sites in genomic sequences is a crucial step for discovering biol...
Modern computational methods are revealing putative transcription-factor (TF) binding sites at an ex...
This chapter describes two-dimensional protein electrophoresis in phylogenetic studies. For molecula...
We applied phage display technology to DNA-protein interaction studies. A cDNA expression library di...
Abstract Background In a traditional electrophoresis mobility shift assay (EMSA) a 32P-labeled doubl...
We applied phage display technology to DNA-protein interaction studies. A cDNA expression library di...
Transcription factor-DNA interactions are some of the most important processes in biology because th...
We have used two-dimensional gel electrophoresis as a general „preparative” method to purify protein...
A novel strategy has been used to isolate a cDNA clone that encodes a DNA binding domain whose recog...
Phage display is a useful means of identifying and selecting proteins of interest that bind specific...
The aim of the work described in this thesis was to identify and characterise novel genes in the cla...
The integration host factor (IHF) of Escherichia coli is a small, sequence-specific DNA-binding prot...
The study of molecular recognition of DNA by natural and synthetic ligands has made enormous progres...
Transcription factors lie at the center of gene regulation, and their identification is crucial to t...
A method to detect DNA-binding sites on the surface of a protein structure is important for func-tio...
Recognition of protein-DNA binding sites in genomic sequences is a crucial step for discovering biol...
Modern computational methods are revealing putative transcription-factor (TF) binding sites at an ex...
This chapter describes two-dimensional protein electrophoresis in phylogenetic studies. For molecula...