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W Bujalowski

Showing results (1-10 of 52) with videos related to

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Biophysical Chemistry|June 1, 1988
Contributions to selective binding of aromatic amino acid residues to tRNA(Phe)W Bujalowski, D Porschke
Nucleic Acids Research|October 11, 1984
Selective binding of amino acid residues to tRNAPheW Bujalowski, D Porschke
Zeitschrift Fur Naturforschung. C, Journal of Biosciences|January 1, 1988
Selective binding of amino acid residues to tRNA molecules detected by anticodon-anticodon interactionsW Bujalowski, D Porschke
Biophysical Chemistry|February 28, 1997
Quantitative analysis of ligand-macromolecule interactions using differential dynamic quenching of the ligand fluorescence to monitor the bindingM J Jezewska, W Bujalowski
Biochemistry|May 24, 1994
Effects of base composition on the negative cooperativity and binding mode transitions of Escherichia coli SSB-single-stranded DNA complexesT M Lohman, W Bujalowski
Biochemistry|April 5, 1988
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 modesT M Lohman, W Bujalowski
Journal of Molecular Biology|May 5, 1989
Negative co-operativity in Escherichia coli single strand binding protein-oligonucleotide interactions. I. Evidence and a quantitative modelW Bujalowski, T M Lohman
Biochemistry|February 24, 2000
Kinetic mechanism of nucleotide cofactor binding to Escherichia coli replicative helicase DnaB protein. stopped-flow kinetic studies using fluorescent, ribose-, and base-modified nucleotide analoguesW Bujalowski, M J Jezewska
Biochemistry|April 19, 1994
Structural characteristics of the nucleotide-binding site of Escherichia coli primary replicative helicase DnaB protein. Studies with ribose and base-modified fluorescent nucleotide analogsW Bujalowski, M M Klonowska
Biochemistry|June 2, 1987
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 interactionsW Bujalowski, T M Lohman
Pageof 6

Showing results (1-10 of 52) with videos related to

Sort By:
Pageof 6
Biophysical Chemistry|June 1, 1988
Contributions to selective binding of aromatic amino acid residues to tRNA(Phe)W Bujalowski, D Porschke
Nucleic Acids Research|October 11, 1984
Selective binding of amino acid residues to tRNAPheW Bujalowski, D Porschke
Zeitschrift Fur Naturforschung. C, Journal of Biosciences|January 1, 1988
Selective binding of amino acid residues to tRNA molecules detected by anticodon-anticodon interactionsW Bujalowski, D Porschke
Biophysical Chemistry|February 28, 1997
Quantitative analysis of ligand-macromolecule interactions using differential dynamic quenching of the ligand fluorescence to monitor the bindingM J Jezewska, W Bujalowski
Biochemistry|May 24, 1994
Effects of base composition on the negative cooperativity and binding mode transitions of Escherichia coli SSB-single-stranded DNA complexesT M Lohman, W Bujalowski
Biochemistry|April 5, 1988
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 modesT M Lohman, W Bujalowski
Journal of Molecular Biology|May 5, 1989
Negative co-operativity in Escherichia coli single strand binding protein-oligonucleotide interactions. I. Evidence and a quantitative modelW Bujalowski, T M Lohman
Biochemistry|February 24, 2000
Kinetic mechanism of nucleotide cofactor binding to Escherichia coli replicative helicase DnaB protein. stopped-flow kinetic studies using fluorescent, ribose-, and base-modified nucleotide analoguesW Bujalowski, M J Jezewska
Biochemistry|April 19, 1994
Structural characteristics of the nucleotide-binding site of Escherichia coli primary replicative helicase DnaB protein. Studies with ribose and base-modified fluorescent nucleotide analogsW Bujalowski, M M Klonowska
Biochemistry|June 2, 1987
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 interactionsW Bujalowski, T M Lohman
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