Thermodynamic Analysis of Ligand-Induced Changes in Protein Thermal Unfolding Applied to High-Throughput Determination of Ligand Affinities with Extrinsic Fluorescent Dyes-Reference-Cited by-同舟云学术

Thermodynamic Analysis of Ligand-Induced Changes in Protein Thermal Unfolding Applied to High-Throughput Determination of Ligand Affinities with Extrinsic Fluorescent Dyes

Published:2010-12-03 Issue:51 Volume:49 Page:10831-10841
ISSN:0006-2960
Container-title:Biochemistry
language:en
Short-container-title:Biochemistry

Author:

Layton Curtis J.¹,Hellinga Homme W.¹

Affiliation:

1. Department of Biochemistry, Duke University Medical Center, Durham, North Carolina 27710, United States

Publisher

American Chemical Society (ACS)

Subject

Biochemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/bi101414z

Reference46 articles.

1. Study of strong to ultratight protein interactions using differential scanning calorimetry

2. High-Density Miniaturized Thermal Shift Assays as a General Strategy for Drug Discovery

3. Evaluation of fluorescence-based thermal shift assays for hit identification in drug discovery

4. Thermodynamic Stability of Carbonic Anhydrase: Measurements of Binding Affinity and Stoichiometry Using ThermoFluor

5. A Quantitative Model of Thermal Stabilization and Destabilization of Proteins by Ligands

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