Bio-layer Interferometry for Measuring Kinetics of Protein-protein Interactions and Allosteric Ligand Effects

Bio-layer interferometry for measuring kinetics of protein-protein interactions and allosteric ligand effects.

We describe the use of Bio-layer Interferometry to study inhibitory interactions of subunit ε with the catalytic complex of Escherichia coli ATP synthase. Bacterial F-type ATP synthase is the target of a new, FDA-approved antibiotic to combat drug-resistant tuberculosis. Understanding bacteria-specific auto-inhibition of ATP synthase by the C-terminal domain of subunit ε could provide a new mea...

Measuring protein-protein interactions.

The binding of one protein to another provokes a variety of biophysical changes that can then be used as a measure of the binding reaction. Optical spectroscopy, particularly fluorescence, is the most flexible technique, but surface plasmon resonance biosensors, microcalorimetry and mass spectroscopy have recently shown significant development.

[Methods for analysis of protein-protein and protein-ligand interactions].

In order to maintain cellular homeostasis, cellular proteins coexist in complex and variable molecular assemblies. Therefore, understanding of major physiological processes at molecular level is based on analysis of protein-protein interaction networks. Firstly, composition of the molecular assembly has to be qualitatively analyzed. In the next step, quantitative bio-chemical properties of the ...

Optical methods for measuring protein-protein interactions.

The hepatopancreas protein, therefore, probably represents the membranous proton channel of the vacuolar ATPase and electron microscopy has given us the clearest impression yet of its organization; an organization clearly consistent with the functional characteristics of the chloroplast ATPase-CF,, complex [22]. It is hoped that techniques such as electron diffraction may improve the structural...

Protein Ligand Interactions