Stopped-Flow Fluorescence Studies of HMG-Domain Protein Binding to Cisplatin-Modified DNA†

Biochemistry ◽  
2000 ◽  
Vol 39 (29) ◽  
pp. 8426-8438 ◽  
Author(s):  
Elizabeth R. Jamieson ◽  
Stephen J. Lippard
Keyword(s):  
Protein Binding ◽  
Stopped Flow ◽  
Fluorescence Studies ◽  
Modified Dna ◽  
Domain Protein

Stopped-flow studies on drug-protein binding

1980 ◽  
Vol 313 (3) ◽  
pp. 269-274 ◽  
Author(s):  
N. Rietbrock ◽  
A. La�mann
Keyword(s):  
Protein Binding ◽  
Stopped Flow ◽  
Drug Protein Binding

Stopped-flow fluorescence studies on binding of snake neurotoxins to acetylcholine receptor

1987 ◽  
Vol 6 (3) ◽  
Author(s):  
Toshiya Endo ◽  
Mamoru Nakanishi ◽  
Shoei Furukawa ◽  
FrancoisJ. Joubert ◽  
Nobuo Tamiya ◽  
...  
Keyword(s):  
Acetylcholine Receptor ◽  
Stopped Flow ◽  
Fluorescence Studies ◽  
Snake Neurotoxins

SH3 Domain Protein-Binding Arrays

2004 ◽  
pp. 183-190
Author(s):  
Sangpen Chamnongpol ◽  
Xianqiang Li
Keyword(s):  
Protein Binding ◽  
Sh3 Domain ◽  
Domain Protein

scholarly journals Investigation of the effect of metal ions on the reactivity of thiol groups in human 5-aminolaevulinate dehydratase

1985 ◽  
Vol 225 (3) ◽  
pp. 573-580 ◽  
Author(s):  
P N B Gibbs ◽  
M G Gore ◽  
P M Jordan
Keyword(s):  
Metal Ions ◽  
Binding Sites ◽  
The Other ◽  
Stopped Flow ◽  
Thiol Groups ◽  
Protein Fluorescence ◽  
Fluorescence Studies ◽  
Nitrobenzoic Acid ◽  
Rate Of Reaction ◽  
Molar Equivalent

The reaction of human 5-aminolaevulinate dehydratase with 5,5′-dithiobis-(2-nitrobenzoic acid) (Nbs2) results in the release of 4 molar equivalents of 5-mercapto-2-nitrobenzoic acid (Nbs) per subunit. Two of the thiol groups reacted very rapidly (groups I and II), and their rate constants were determined by stopped-flow spectrophotometry; the other two thiol groups (groups III and IV) were observed by conventional spectroscopy. Titration of the enzyme with a 1 molar equivalent concentration of Nbs2 resulted in the release of 2 molar equivalents of Nbs and the concomitant formation of an intramolecular disulphide bond between groups I and II. Removal of zinc from the holoenzyme increased the reactivity of groups I and II without significantly affecting the rate of reaction of the other groups. The reactions of the thiol groups in both the holoenzyme and apoenzyme were little affected by the presence of Pb2+ ions at concentrations that strongly inhibit the enzyme, suggesting that Zn2+ and Pb2+ ions may have independent binding sites. Protein fluorescence studies with Pb2+ and Zn2+ have shown that the binding of both metal ions results in perturbation of the protein fluorescence.

Stopped-flow studies on drug-protein binding

1982 ◽  
Vol 320 (2) ◽  
pp. 189-195 ◽  
Author(s):  
A. La�mann ◽  
N. Rietbrock
Keyword(s):  
Protein Binding ◽  
Stopped Flow ◽  
Drug Protein Binding
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