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Spectroscopy: An International Journal
Volume 27 (2012), Article ID 745136, 4 pages

THz and IR Spectroscopy of Molecular Systems That Simulate Function-Related Structural Changes of Proteins

1Faculty of Physics and International Laser Center, Moscow State University, Moscow 119991, Russia
2Faculty of Chemistry, Moscow State University, Moscow 119991, Russia

Copyright © 2012 N. N. Brandt et al. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.


The activity of enzymes in organic solvents substantially increases in the presence of crown ethers. Tris(hydroxymethyl)aminomethane (tris) is chosen as a model compound to simulate the interaction of surface amino groups of proteins with crown ether. The methods of FTIR and time-domain THz spectroscopy are used to study the interaction of tris with 18-crown-6. The THz spectra of the complexes are measured for the first time.