Thermodynamic and kinetic methods of analyses of protein-nucleic acid interactions. From simpler to more complex systems

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Abstract

This review describes the thermodynamically rigorous analyses of spectroscopic approaches to study protein-nucleic acid interactions, including multiple-ligand binding phenomena to obtain model-independent binding isotherms and the analyses of spectroscopic stopped-flow kinetic approaches used to examine mechanisms of protein-nucleic acid interactions with emphasis on the properties of the reaction intermediates. The discussion focuses on the fundamental problem of obtaining thermodynamic, spectroscopic, and kinetic parameters free of assumptions about the relationship between the observed signal and the degree of protein or nucleic acid saturation. Topics discussed include the direct versus indirect methods in studying protein-nucleic acid interactions and the thermodynamic bases of quantitative equilibrium spectroscopic titrations.

Original languageEnglish (US)
Pages (from-to)556-606
Number of pages51
JournalChemical Reviews
Volume106
Issue number2
DOIs
StatePublished - Feb 2006

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Nucleic Acids
Large scale systems
Thermodynamics
Kinetics
Proteins
Reaction intermediates
Titration
Kinetic parameters
Isotherms
Ligands

ASJC Scopus subject areas

  • Chemistry(all)

Cite this

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abstract = "This review describes the thermodynamically rigorous analyses of spectroscopic approaches to study protein-nucleic acid interactions, including multiple-ligand binding phenomena to obtain model-independent binding isotherms and the analyses of spectroscopic stopped-flow kinetic approaches used to examine mechanisms of protein-nucleic acid interactions with emphasis on the properties of the reaction intermediates. The discussion focuses on the fundamental problem of obtaining thermodynamic, spectroscopic, and kinetic parameters free of assumptions about the relationship between the observed signal and the degree of protein or nucleic acid saturation. Topics discussed include the direct versus indirect methods in studying protein-nucleic acid interactions and the thermodynamic bases of quantitative equilibrium spectroscopic titrations.",
author = "Wlodzimierz Bujalowski",
year = "2006",
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AB - This review describes the thermodynamically rigorous analyses of spectroscopic approaches to study protein-nucleic acid interactions, including multiple-ligand binding phenomena to obtain model-independent binding isotherms and the analyses of spectroscopic stopped-flow kinetic approaches used to examine mechanisms of protein-nucleic acid interactions with emphasis on the properties of the reaction intermediates. The discussion focuses on the fundamental problem of obtaining thermodynamic, spectroscopic, and kinetic parameters free of assumptions about the relationship between the observed signal and the degree of protein or nucleic acid saturation. Topics discussed include the direct versus indirect methods in studying protein-nucleic acid interactions and the thermodynamic bases of quantitative equilibrium spectroscopic titrations.

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