Ontology highlight
ABSTRACT:
SUBMITTER: Groftehauge MK
PROVIDER: S-EPMC4304684 | biostudies-literature | 2015 Jan
REPOSITORIES: biostudies-literature
Acta crystallographica. Section D, Biological crystallography 20150101 Pt 1
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 ...[more]