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Protein–ligand interactions investigated by thermal shift assays (TSA) and dual polarization interferometry (DPI)

Grøftehauge, Morten K.; Hajizadeh, Nelly R.; Swann, Marcus J.; Pohl, Ehmke

Authors

Morten K. Grøftehauge

Nelly R. Hajizadeh

Marcus J. Swann



Abstract

Over the last decades, a wide range of biophysical techniques investigating protein-ligand interactions have become indispensable tools to complement high-resolution crystal structure determinations. Current approaches in solution range from high-throughput-capable methods such as thermal shift assays (TSA) to highly accurate techniques including microscale thermophoresis (MST) and isothermal titration calorimetry (ITC) that can provide a full thermodynamic description of binding events. Surface-based methods such as surface plasmon resonance (SPR) and dual polarization interferometry (DPI) allow real-time measurements and can provide kinetic parameters as well as binding constants. DPI provides additional spatial information about the binding event. Here, an account is presented of new developments and recent applications of TSA and DPI connected to crystallography.

Citation

Grøftehauge, M. K., Hajizadeh, N. R., Swann, M. J., & Pohl, E. (2015). Protein–ligand interactions investigated by thermal shift assays (TSA) and dual polarization interferometry (DPI). Acta crystallographica. Section D, Biological crystallography, 71(1), 36-44. https://doi.org/10.1107/s1399004714016617

Journal Article Type Article
Acceptance Date Jul 17, 2014
Online Publication Date Jan 1, 2015
Publication Date 2015-01
Deposit Date Sep 5, 2017
Journal Acta crystallographica . Section D, Biological crystallography
Print ISSN 0907-4449
Electronic ISSN 1399-0047
Publisher Blackwell
Peer Reviewed Peer Reviewed
Volume 71
Issue 1
Pages 36-44
DOI https://doi.org/10.1107/s1399004714016617