Quantitative Thermodynamic Analyses of Spectroscopic Titration Curves.

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Cooperativity in Binding Processes: New Insights from Phenomenological Modeling Evidence of Kinetic Cooperativity in Dimeric Ketopantoate Reductase from Staphylococcus aureus.A Note on the use of Steady-State Fluorescence Quenching to Quantify Nanoparticle-Protein Interactions.

P2860

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P2860

Quantitative Thermodynamic Analyses of Spectroscopic Titration Curves.

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http://www.wikidata.org/entity/Q42025314

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2014 nî lūn-bûn

@nan

2014年の論文

@ja

2014年論文

@yue

2014年論文

@zh-hant

2014年論文

@zh-hk

2014年論文

@zh-mo

2014年論文

@zh-tw

2014年论文

@wuu

2014年论文

@zh

2014年论文

@zh-cn

name

Quantitative Thermodynamic Analyses of Spectroscopic Titration Curves.

@en

Quantitative Thermodynamic Analyses of Spectroscopic Titration Curves.

@nl

type

Item

label

Quantitative Thermodynamic Analyses of Spectroscopic Titration Curves.

@en

Quantitative Thermodynamic Analyses of Spectroscopic Titration Curves.

@nl

prefLabel

Quantitative Thermodynamic Analyses of Spectroscopic Titration Curves.

@en

Quantitative Thermodynamic Analyses of Spectroscopic Titration Curves.

@nl

P1476

Quantitative Thermodynamic Analyses of Spectroscopic Titration Curves.

@en

P2093

Maria J Jezewska

http://www.w3.org/2001/XMLSchema#string

Wlodzimierz Bujalowski

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P2860

Equilibria and kinetics of lac repressor-operator interactions by polyacrylamide gel electrophoresis

Comparative thermodynamic analysis of DNA--protein interactions using surface plasmon resonance and fluorescence correlation spectroscopy.

A universal thermodynamic approach to analyze biomolecular binding experiments.

Interactions of Escherichia coli primary replicative helicase DnaB protein with nucleotide cofactors.

Interactions of the Escherichia coli DnaB-DnaC protein complex with nucleotide cofactors. 1. Allosteric conformational transitions of the complex.

Full-length Dengue virus RNA-dependent RNA polymerase-RNA/DNA complexes: stoichiometries, intrinsic affinities, cooperativities, base, and conformational specificities.

A double-filter method for nitrocellulose-filter binding: application to protein-nucleic acid interactions.

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

Limited co-operativity in protein-nucleic acid interactions. A thermodynamic model for the interactions of Escherichia coli single strand binding protein with single-stranded nucleic acids in the "beaded", (SSB)65 mode.

Application of fluorescence energy transfer and polarization to monitor Escherichia coli cAMP receptor protein and lac promoter interaction

P304

40-50

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P31

scholarly article

P356

10.1016/J.MOLSTRUC.2014.04.041

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P478

1077

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P577

2014-12-01T00:00:00Z

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P698

25284889

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P932

4181404

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Quantitative Thermodynamic Analyses of Spectroscopic Titration Curves.

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P2860

P2860

Quantitative Thermodynamic Analyses of Spectroscopic Titration Curves.

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name

type

label

prefLabel

P1433

P1476

P2093

P2860

P304

P31

P356

P478

P577

P698

P932

P356

P1433

P1476

P2093

P2860

P304

P31

P356

P478

P577

P698

P932