Work

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

Year: 2014

Type: article

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.

Source: Acta Crystallographica Section D Biological Crystallography

DOI: 10.1107/s1399004714016617

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

Institutions: Durham University, Biolin Scientific (United Kingdom)

Language: English

Topic: thermodynamics and calorimetric analyses

Subfield: Physical and Theoretical Chemistry

Field: Chemistry

Domain: Physical Sciences

Open Access status: hybrid

Estimated APC paid: $4,740

Funder: Wellcome Trust