Using Lamm-Equation modeling of sedimentation velocity data to determine the kinetic and thermodynamic properties of macromolecular interactions (Q33780814)

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English	Using Lamm-Equation modeling of sedimentation velocity data to determine the kinetic and thermodynamic properties of macromolecular interactions	scientific article

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scholarly article

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Europe PubMed Central

29 July 2017

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Europe PubMed Central

Using Lamm-Equation modeling of sedimentation velocity data to determine the kinetic and thermodynamic properties of macromolecular interactions (English)

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Europe PubMed Central

29 July 2017

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based on heuristic

inferred from title

Chad A Brautigam

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Chad A Brautigam

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Europe PubMed Central

29 July 2017

language of work or name

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based on heuristic

inferred from title

publication date

25 December 2010

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Europe PubMed Central

29 July 2017

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Europe PubMed Central

29 July 2017

54

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Europe PubMed Central

29 July 2017

1

1 reference

Europe PubMed Central

29 July 2017

4-15

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Europe PubMed Central

29 July 2017

Determination of protein complex stoichiometry through multisignal sedimentation velocity experiments.

1 reference

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Sedimentation patterns of rapidly reversible protein interactions.

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https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pmc&linkname=pmc_refs_pubmed&retmode=json&id=3147155

4 July 2018

On the analysis of sedimentation velocity in the study of protein complexes

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Subunit and catalytic component stoichiometries of an in vitro reconstituted human pyruvate dehydrogenase complex

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Hierarchical regulation of WASP/WAVE proteins

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1 reference

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Analysis of heterologous interacting systems by sedimentation velocity: curve fitting algorithms for estimation of sedimentation coefficients, equilibrium and kinetic constants.

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Global analysis of non-specific protein-nucleic interactions by sedimentation equilibrium

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On the analysis of protein self-association by sedimentation velocity analytical ultracentrifugation

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Size-distribution analysis of proteins by analytical ultracentrifugation: strategies and application to model systems

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Non-ideality by sedimentation velocity of halophilic malate dehydrogenase in complex solvents

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Size-Distribution Analysis of Macromolecules by Sedimentation Velocity Ultracentrifugation and Lamm Equation Modeling

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Calculation of hydrodynamic properties of globular proteins from their atomic-level structure

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Direct sedimentation analysis of interference optical data in analytical ultracentrifugation

1 reference

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Sedimentation analysis of noninteracting and self-associating solutes using numerical solutions to the Lamm equation

1 reference

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Molecular mass determination by sedimentation velocity experiments and direct fitting of the concentration profiles

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The effect of self-association on the interaction of the Escherichia coli regulatory protein TyrR with DNA.

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SOMO (SOlution MOdeler) differences between X-Ray- and NMR-derived bead models suggest a role for side chain flexibility in protein hydrodynamics.

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1 reference

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Sedimentation of generalized systems of interacting particles. I. Solution of systems of complete Lamm equations

1 reference

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30 October 2018

The analysis of macromolecular interactions by sedimentation equilibrium

1 reference

https://api.crossref.org/works/10.1016%2FJ.YMETH.2010.12.029

7 January 2021

Evaluating the stoichiometry of macromolecular complexes using multisignal sedimentation velocity.

1 reference

https://api.crossref.org/works/10.1016%2FJ.YMETH.2010.12.029

7 January 2021

Boundary Problems in the Sedimentation and Electrophoresis of Complex Systems in Rapid Reversible Equilibrium

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The boundary structure in the analysis of reversibly interacting systems by sedimentation velocity

1 reference

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7 January 2021

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10.1016/J.YMETH.2010.12.029

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Europe PubMed Central

29 July 2017

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Europe PubMed Central

29 July 2017

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Europe PubMed Central

29 July 2017

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