scholarly journals Cooperative kinetics of ligand binding to linear polymers

2022 ◽  
Author(s):  
Juan P.G. Villaluenga ◽  
Francisco Javier Cao-García
Keyword(s):  
Ligand Binding ◽  
Linear Polymers ◽  
Kinetics Of ◽  
Cooperative Kinetics

Arrangement Of Monomeric Units In Fibrin

1979 ◽  
Author(s):  
Jan Hermans
Keyword(s):  
Fiber Axis ◽  
High Symmetry ◽  
Linear Polymers ◽  
Fiber Volume ◽  
High Fiber ◽  
Rotation Axes ◽  
Small Set ◽  
Helical Turn ◽  
The One ◽  
Kinetics Of

Measurements of light scattering have given much information about formation and properties of fibrin. These studies have determined mass-length ratio of linear polymers (protofibrils) and of fibers, kinetics of polymerization and of lateral association and volume-mass ratio of thick fibers. This ratio is 5 to 1. On the one hand, this high value suggests that the fiber contains channels that allow the diffusion of enzymes such as Factor XHIa and plasmin; on the other hand, the high value appears paradoxical for a stiff fiber made up of elongated units (fibrin monomers) arranged in parallel. Such a high fiber volume is a property of only a small set out of many high-symmetry models of fibrin, which may be constructed from overlapping three-domain monomers which are arranged into strands, are aligned nearly parallel to the fiber axis and make adequate longitudinal and lateral contacts. These models contain helical protofibrils related to each other by rotation axes parallel to the fiber axis. The protofibrils may contain 2, 3 or 4 monomers per helical turn and there are four possible symmetries. A large specific volume is achieved if the ends of each monomer are slightly displaced from the protofibril axis, either by a shift or by a tilt of the monomer. The fiber containing tilted monomers is more highly interconnected; the two ends of a tilted monomer form lateral contacts with different adjacent protofibrils, whereas the two ends of a non-tilted monomer contact the same adjacent protofibril(s).

scholarly journals The Kinetics of Ligand Binding and of the Association-Dissociation Reactions of Human Hemoglobin

1971 ◽  
Vol 246 (9) ◽  
pp. 2796-2807 ◽  
Author(s):  
Melvin E. Andersen ◽  
J. Keith Moffat ◽  
Quentin H. Gibson
Keyword(s):  
Ligand Binding ◽  
Human Hemoglobin ◽  
Kinetics Of

scholarly journals Electrostatic influence on the kinetics of ligand binding to acetylcholinesterase. Distinctions between active center ligands and fasciculin.

1998 ◽  
Vol 273 (19) ◽  
pp. 11986
Author(s):  
Zoran Radic ◽  
Paul D. Kirchhoff ◽  
Daniel M. Quinn ◽  
J. Andrew McCammon ◽  
Palmer Taylor
Keyword(s):  
Ligand Binding ◽  
Active Center ◽  
Kinetics Of

scholarly journals Equilibria and Kinetics of Ligand Binding by Leghemoglobin from Soybean Root Nodules

1972 ◽  
Vol 247 (2) ◽  
pp. 521-526
Author(s):  
Takashi Imamura ◽  
Austen Riggs ◽  
Quentin H. Gibson
Keyword(s):  
Ligand Binding ◽  
Root Nodules ◽  
Soybean Root ◽  
Kinetics Of

scholarly journals Kinetics of ligand binding to Pseudoterranova decipiens and Ascaris suum hemoglobins and to Leu-29–>Tyr sperm whale myoglobin mutant

1993 ◽  
Vol 268 (23) ◽  
pp. 16993-16998
Author(s):  
Q.H. Gibson ◽  
R. Regan ◽  
J.S. Olson ◽  
T.E. Carver ◽  
B. Dixon ◽  
...  
Keyword(s):  
Ligand Binding ◽  
Ascaris Suum ◽  
Sperm Whale ◽  
Pseudoterranova Decipiens ◽  
Kinetics Of ◽  
Sperm Whale Myoglobin

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.

scholarly journals Live Cell Imaging Of The Kinetics Of Ligand Binding At The Human Adenosine A3 Receptor

2009 ◽  
Vol 96 (3) ◽  
pp. 677a
Author(s):  
Lauren T. May ◽  
Stephen J. Briddon ◽  
Stephen J. Hill
Keyword(s):  
Ligand Binding ◽  
Live Cell Imaging ◽  
Cell Imaging ◽  
Live Cell ◽  
Adenosine A3 Receptor ◽  
Kinetics Of

Kinetics of Ligand Binding to Aquocobalamin*

Biochemistry ◽  
1967 ◽  
Vol 6 (5) ◽  
pp. 1520-1525 ◽  
Author(s):  
W. C. Randall ◽  
R. A. Alberty
Keyword(s):  
Ligand Binding ◽  
Kinetics Of
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