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Updated: Mar 2, 2026

Bio-layer Interferometry for Measuring Kinetics of Protein-protein Interactions and Allosteric Ligand Effects
Published on: February 18, 2014
Terahertz optical measurements of correlated motions with possible allosteric function
Katherine A Niessen1, Mengyang Xu1, A G Markelz2
1Department of Physics, University at Buffalo (SUNY), Buffalo, NY, 14260, USA.
Abstract:
A suggested mechanism for allosteric response is the distortion of the energy landscape with agonist binding changing the protein structure's access to functional configurations. Intramolecular vibrations are indicative of the energy landscape and may have trajectories that enable functional conformational change. Here, we discuss the development of an optical method to measure the intramolecular vibrations in proteins, namely, crystal anisotropy terahertz microscopy, and the various approaches which can be used to identify the spectral data with specific structural motions.
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