Determination of Equilibrium binding constants for LPS interaction with TLR4

[15] Determination of rate and equilibrium binding constants for macromolecular interactions by surface plasmon resonance

Part B: Numerical Computer Methods - Methods in Enzymology ◽

10.1016/s0076-6879(94)40054-7 ◽

1994 ◽

pp. 323-349 ◽

Cited By ~ 47

Author(s):

Daniel J. O'Shannessy ◽

Michael Brigham-Burke ◽

K. Karl Soneson ◽

Preston Hensley ◽

Ian Brooks

Keyword(s):

Surface Plasmon Resonance ◽

Surface Plasmon ◽

Plasmon Resonance ◽

Binding Constants ◽

Equilibrium Binding ◽

Macromolecular Interactions

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Determination of kinetic rate and equilibrium binding constants for macromolecular interactions: a critique of the surface plasmon resonance literature

Current Opinion in Biotechnology ◽

10.1016/s0958-1669(05)80072-2 ◽

1994 ◽

Vol 5 (1) ◽

pp. 65-71 ◽

Cited By ~ 102

Author(s):

Daniel J O'Shannessy

Keyword(s):

Surface Plasmon Resonance ◽

Surface Plasmon ◽

Plasmon Resonance ◽

Binding Constants ◽

Kinetic Rate ◽

Equilibrium Binding ◽

Macromolecular Interactions

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Generally Applicable NMR Titration Methods for the Determination of Equilibrium Constants for Coordination Complexes: Syntheses and Characterizations of Metallacrown Ethers with α,ω-Bis(phosphite)-polyether Ligands and Determination of Equilibrium Binding Constants to Li+

Organometallics ◽

10.1021/om200580t ◽

2011 ◽

Vol 30 (21) ◽

pp. 5695-5709 ◽

Cited By ~ 16

Author(s):

Justin T. Sheff ◽

Aaron L. Lucius ◽

Sam B. Owens ◽

Gary M. Gray

Keyword(s):

Equilibrium Constants ◽

Binding Constants ◽

Coordination Complexes ◽

Nmr Titration ◽

Metallacrown Ethers ◽

Equilibrium Binding

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Structural requirements of tetracycline-Tet repressor interaction: determination of equilibrium binding constants for tetracycline analogs with the Tet repressor.

Antimicrobial Agents and Chemotherapy ◽

10.1128/aac.35.8.1591 ◽

1991 ◽

Vol 35 (8) ◽

pp. 1591-1595 ◽

Cited By ~ 63

Author(s):

J Degenkolb ◽

M Takahashi ◽

G A Ellestad ◽

W Hillen

Keyword(s):

Binding Constants ◽

Structural Requirements ◽

Equilibrium Binding ◽

Tet Repressor

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Determination of Receptor-Ligand Kinetic and Equilibrium Binding Constants using Surface Plasmon Resonance: Application to the lck SH2 Domain and Phosphotyrosyl Peptides

Journal of Medicinal Chemistry ◽

10.1021/jm00008a009 ◽

1995 ◽

Vol 38 (8) ◽

pp. 1309-1318 ◽

Cited By ~ 53

Author(s):

M. M. Morelock ◽

R. H. Ingraham ◽

R. Betageri ◽

S. Jakes

Keyword(s):

Surface Plasmon Resonance ◽

Surface Plasmon ◽

Plasmon Resonance ◽

Binding Constants ◽

Sh2 Domain ◽

Receptor Ligand ◽

Equilibrium Binding

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Determination of Rate and Equilibrium Binding Constants for Macromolecular Interactions Using Surface Plasmon Resonance: Use of Nonlinear Least Squares Analysis Methods

Analytical Biochemistry ◽

10.1006/abio.1993.1355 ◽

1993 ◽

Vol 212 (2) ◽

pp. 457-468 ◽

Cited By ~ 382

Author(s):

D.J. Oshannessy ◽

M. Brighamburke ◽

K.K. Soneson ◽

P. Hensley ◽

I. Brooks

Keyword(s):

Surface Plasmon Resonance ◽

Least Squares ◽

Surface Plasmon ◽

Plasmon Resonance ◽

Binding Constants ◽

Nonlinear Least Squares ◽

Equilibrium Binding ◽

Macromolecular Interactions ◽

Analysis Methods

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Faculty Opinions recommendation of Determination of protein-ligand binding constants of a cooperatively regulated tetrameric enzyme using electrospray mass spectrometry.

Faculty Opinions – Post-Publication Peer Review of the Biomedical Literature ◽

10.3410/f.718145671.793488431 ◽

2013 ◽

Author(s):

Thomas Kodadek ◽

Xiaodan Liu

Keyword(s):

Mass Spectrometry ◽

Ligand Binding ◽

Electrospray Mass Spectrometry ◽

Binding Constants

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Determination of Enzyme or Binding Constants Using Generalized Linear Models, with Particular Reference to Michaelis–Menten Models

Journal of Pharmaceutical Sciences ◽

10.1002/jps.2600780514 ◽

1989 ◽

Vol 78 (5) ◽

pp. 413-416

Author(s):

Gerald Van Belle ◽

Sue Leurgans ◽

Pat Friel ◽

Sunwei Guo ◽

Mark Yerby

Keyword(s):

Generalized Linear Models ◽

Linear Models ◽

Binding Constants

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Kinetic mechanism of Na+-coupled aspartate transport catalyzed by GltTk

Communications Biology ◽

10.1038/s42003-021-02267-y ◽

2021 ◽

Vol 4 (1) ◽

Author(s):

Gianluca Trinco ◽

Valentina Arkhipova ◽

Alisa A. Garaeva ◽

Cedric A. J. Hutter ◽

Markus A. Seeger ◽

...

Keyword(s):

Kinetic Mechanism ◽

Protein Quantification ◽

Detergent Solution ◽

Sodium Ions ◽

Binding Studies ◽

Equilibrium Binding ◽

Uptake Rates ◽

Bona Fide ◽

Inside Out

AbstractIt is well-established that the secondary active transporters GltTk and GltPh catalyze coupled uptake of aspartate and three sodium ions, but insight in the kinetic mechanism of transport is fragmentary. Here, we systematically measured aspartate uptake rates in proteoliposomes containing purified GltTk, and derived the rate equation for a mechanism in which two sodium ions bind before and another after aspartate. Re-analysis of existing data on GltPh using this equation allowed for determination of the turnover number (0.14 s−1), without the need for error-prone protein quantification. To overcome the complication that purified transporters may adopt right-side-out or inside-out membrane orientations upon reconstitution, thereby confounding the kinetic analysis, we employed a rapid method using synthetic nanobodies to inactivate one population. Oppositely oriented GltTk proteins showed the same transport kinetics, consistent with the use of an identical gating element on both sides of the membrane. Our work underlines the value of bona fide transport experiments to reveal mechanistic features of Na+-aspartate symport that cannot be observed in detergent solution. Combined with previous pre-equilibrium binding studies, a full kinetic mechanism of structurally characterized aspartate transporters of the SLC1A family is now emerging.

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