Size-Dependent Relationships between Protein Stability and Thermal Unfolding Temperature Have Important Implications for Analysis of Protein Energetics and High-Throughput Assays of Protein–Ligand Interactions-Reference-Cited by-同舟云学术

Size-Dependent Relationships between Protein Stability and Thermal Unfolding Temperature Have Important Implications for Analysis of Protein Energetics and High-Throughput Assays of Protein–Ligand Interactions

Published:2017-08-14 Issue:21 Volume:122 Page:5278-5285
ISSN:1520-6106
Container-title:The Journal of Physical Chemistry B
language:en
Short-container-title:J. Phys. Chem. B

Author:

Watson Matthew D.,Monroe Jeremy,Raleigh Daniel P.¹^ORCID

Affiliation:

1. Research Department of Structural and Molecular Biology, University College London, Gower Street, London, WC1E 6BT, United Kingdom

Funder

Division of Molecular and Cellular Biosciences

Publisher

American Chemical Society (ACS)

Subject

Materials Chemistry,Surfaces, Coatings and Films,Physical and Theoretical Chemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/acs.jpcb.7b05684

Reference82 articles.

1. Some thermodynamic implications for the thermostability of proteins

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

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

5. Monitoring Drug Target Engagement in Cells and Tissues Using the Cellular Thermal Shift Assay

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