Microscale thermophoresis quantifies biomolecular interactions under previously challenging conditions

• Published in: Methods (San Diego, Calif.) Vol. 59; no. 3; pp. 301 - 315
• Main Authors: Seidel, Susanne A.I., Dijkman, Patricia M., Lea, Wendy A., van den Bogaart, Geert, Jerabek-Willemsen, Moran, Lazic, Ana, Joseph, Jeremiah S., Srinivasan, Prakash, Baaske, Philipp, Simeonov, Anton, Katritch, Ilia, Melo, Fernando A., Ladbury, John E., Schreiber, Gideon, Watts, Anthony, Braun, Dieter, Duhr, Stefan
• Format: Journal Article
• Language: English
• Published: United States Elsevier Inc 01.03.2013
• Subjects: Animals; beta-Lactamase Inhibitors; beta-Lactamases - chemistry; Binding affinity; Binding, Competitive; Bioliquids; Cooperativity; Dimerization; GRB2 Adaptor Protein - chemistry; Histone-Lysine N-Methyltransferase - chemistry; Label-free; Lasers; Microscale thermophoresis; Molecular Conformation; Protein Binding; Proteins - chemistry; Protozoan Proteins - chemistry; Rats; Receptor, Adenosine A2A - chemistry; Receptors, Neurotensin - chemistry; Spectrometry, Fluorescence - methods; Temperature; Thermodynamics; Binding affinity; Cooperativity; Label-free; Dimerization; Microscale thermophoresis; Bioliquids

► Microscale thermophoresis (MST) quantifies protein–protein binding in cell lysate. ► The KD of Grb2-homodimerization is determined. ► Competitive binding of small molecules and peptides to proteins is analyzed. ► GPCR membrane proteins are characterized using label-free MST. ► Syt1-binding to PIP2...