Involvement of a tryptophan residue in the binding site of Escherichia coli galactose-binding protein

Biochemistry ◽  
1974 ◽  
Vol 13 (5) ◽  
pp. 993-999 ◽  
Author(s):  
Eleanor B. McGowan ◽  
Thomas J. Silhavy ◽  
Winfried Boos
Keyword(s):  
Escherichia Coli ◽  
Binding Site ◽  
Binding Protein ◽  
Tryptophan Residue

scholarly journals The binding-site sizes of Escherichia coli single-stranded-DNA-binding protein and mammalian replication protein A are 65 and ⩾54 nucleotides respectively

1997 ◽  
Vol 324 (3) ◽  
pp. 957-961 ◽  
Author(s):  
Michael MITAS ◽  
Johanna Y. CHOCK ◽  
Mellisa CHRISTY
Keyword(s):  
Escherichia Coli ◽  
Binding Site ◽  
Binding Sites ◽  
Binding Protein ◽  
Protein A ◽  
Replication Protein A ◽  
Dna Binding Protein ◽  
Replication Protein ◽  
Electrophoretic Mobilities ◽  
Quantitative Analyses

The electrophoretic mobilities of complexes formed with single-stranded (ss) DNA and tetrameric Escherichia colissDNA-binding protein (EcoSSB) or mammalian replication protein A (RPA) were analysed. The electrophoretic mobilities of the complexes in a native polyacrylamide gel increased as the lengths of the DNA increased from 28 to 70 nt, thus revealing paradoxical ‘descending-staircase’ patterns. Increases in the electrophoretic mobilities of EcoSSB·ssDNA complexes were observed when the lengths of the bound DNA were increased by 1 nt. Quantitative analyses of the complexes suggested that the binding-sites sizes of EcoSSB and RPA were 65 and ⩾ 54 nt respectively. The binding-site size for RPA is at least 24 nt larger than previously reported.

ASSOCIATION BEHAVIOUR OF THE OESTRADIOL-BINDING PROTEIN COMPLEX WITH THE NUCLEAR FRACTION

1972 ◽  
Vol 71 (2_Suppla) ◽  
pp. S420-S438 ◽  
Author(s):  
David L. Williams ◽  
Jack Gorski
Keyword(s):  
Binding Site ◽  
Protein Complex ◽  
Binding Protein ◽  
Nuclear Fraction ◽  
Site Saturation ◽  
Total Binding

ABSTRACT A number of studies have been carried out to examine the distribution of the oestradiol-binding protein complex between cytosol and nuclear fractions as a function of total binding site saturation. The results of these studies suggest that each binding protein has one binding site for the hormone. In addition, these studies suggest that the interaction of the oestradiol-binding protein complex with the nucleus involves a large number of low affinity association sites.

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