Rapid scanning stopped-flow absorption studies of the effect on tryptophanase of a change in pH or potassium(1+) ion concentration: evidence for a slow conformational change

1979 ◽  
Vol 101 (8) ◽  
pp. 2218-2219 ◽  
Author(s):  
David S. June ◽  
Barbara Kennedy ◽  
T. H. Pierce ◽  
Sami V. Elias ◽  
Folim Halaka ◽  
...  
Keyword(s):  
Conformational Change ◽  
Ion Concentration ◽  
Stopped Flow ◽  
Absorption Studies ◽  
Rapid Scanning

scholarly journals Positive co-operative binding at two weak lysine-binding sites governs the Glu-plasminogen conformational change

1992 ◽  
Vol 285 (2) ◽  
pp. 419-425 ◽  
Author(s):  
U Christensen ◽  
L Mølgaard
Keyword(s):  
Ligand Binding ◽  
Binding Site ◽  
Conformational Change ◽  
Conformational Changes ◽  
Binding Sites ◽  
High Specificity ◽  
Stopped Flow ◽  
Protein Fluorescence ◽  
Lysine Residues ◽  
Kinetics Of

The kinetics of a series of Glu-plasminogen ligand-binding processes were investigated at pH 7.8 and 25 degrees C (in 0.1 M-NaCl). The ligands include compounds analogous to C-terminal lysine residues and to normal lysine residues. Changes of the Glu-plasminogen protein fluorescence were measured in a stopped-flow instrument as a function of time after rapid mixing of Glu-plasminogen and ligand at various concentrations. Large positive fluorescence changes (approximately 10%) accompany the ligand-induced conformational changes of Glu-plasminogen resulting from binding at weak lysine-binding sites. Detailed studies of the concentration-dependencies of the equilibrium signals and the rate constants of the process induced by various ligands showed the conformational change to involve two sites in a concerted positive co-operative process with three steps: (i) binding of a ligand at a very weak lysine-binding site that preferentially, but not exclusively, binds C-terminal-type lysine ligands, (ii) the rate-determining actual-conformational-change step and (iii) binding of one more lysine ligand at a second weak lysine-binding site that then binds the ligand more tightly. Further, totally independent initial small negative fluorescence changes (approximately 2-4%) corresponding to binding at the strong lysine-binding site of kringle 1 [Sottrup-Jensen, Claeys, Zajdel, Petersen & Magnusson (1978) Prog. Chem. Fibrinolysis Thrombolysis 3, 191-209] were observed for the C-terminal-type ligands. The finding that the conformational change in Glu-plasminogen involves two weak lysine-binding sites indicates that the effect cannot be assigned to any single kringle and that the problem of whether kringle 4 or kringle 5 is responsible for the process resolves itself. Probably kringle 4 and 5 are both participating. The involvement of two lysine binding-sites further makes the high specificity of Glu-plasminogen effectors more conceivable.

Stopped-Flow Ultra-Rapid-Scanning Fourier Transform Infrared Spectroscopy on the Millisecond Time Scale

2010 ◽  
Vol 64 (8) ◽  
pp. 907-911 ◽  
Author(s):  
Matthew L. Reback ◽  
Christopher W. Roske ◽  
Thomas E. Bitterwolf ◽  
Peter R. Griffiths ◽  
Christopher J. Manning
Keyword(s):  
Fourier Transform ◽  
Infrared Spectroscopy ◽  
Fourier Transform Infrared Spectroscopy ◽  
Time Scale ◽  
Fourier Transform Infrared ◽  
Stopped Flow ◽  
Millisecond Time Scale ◽  
Rapid Scanning

Insights into the Mechanism ofPseudomonas dacunhaeAspartate β-Decarboxylase from Rapid-Scanning Stopped-Flow Kinetics

Biochemistry ◽  
2010 ◽  
Vol 49 (24) ◽  
pp. 5066-5073 ◽  
Author(s):  
Robert S. Phillips ◽  
Santiago Lima ◽  
Roman Khristoforov ◽  
Bakthavatsalam Sudararaju
Keyword(s):  
Stopped Flow ◽  
Stopped Flow Kinetics ◽  
Rapid Scanning

scholarly journals Stopped-Flow Kinetic Study on Intermediate of Theophylline Oxidation Reaction via Rapid-Scanning UV/VIS Spectroscopy.

1997 ◽  
Vol 13 (Supplement) ◽  
pp. 475-478 ◽  
Author(s):  
Ke ZHANG ◽  
Houping HUANG ◽  
Xinguo WU ◽  
Ruxiu CAI ◽  
Takashi KORENAGA
Keyword(s):  
Kinetic Study ◽  
Oxidation Reaction ◽  
Stopped Flow ◽  
Vis Spectroscopy ◽  
Rapid Scanning

scholarly journals Association of α-Synuclein with Lipid Vesicles. Stopped-Flow Kinetics of Concerted Binding and Conformational Change

2014 ◽  
Vol 106 (2) ◽  
pp. 248a
Author(s):  
Thomas M. Jovin ◽  
Volodymyr V. Shvadchak ◽  
Remco Siero ◽  
Lisandro J. Falomir-Lockhart ◽  
Vinod Subramaniam
Keyword(s):  
Conformational Change ◽  
Lipid Vesicles ◽  
Stopped Flow ◽  
Stopped Flow Kinetics ◽  
Kinetics Of
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