Special Section on Laser Applications in Life Sciences

Effect of thermal denaturation, inhibition, and cleavage of disulfide bonds on the low-frequency Raman and FTIR spectra of chymotrypsin and albumin

[+] Author Affiliations
Nikolay N. Brandt

Lomonosov Moscow State University, Faculty of Physics, Leninskie gory 1, Moscow, Russia 119991

Andrey Yu Chikishev

International Laser Center, Leninskie gory 1/62, Moscow, Russia 119991

Anna A. Mankova

Lomonosov Moscow State University, Faculty of Physics, Leninskie gory 1, Moscow, Russia 119991

Inna K. Sakodynskaya

Lomonosov Moscow State University, Faculty of Chemistry, Leninskie gory 1, Moscow, Russia 119991

J. Biomed. Opt. 20(5), 051015 (Dec 05, 2014). doi:10.1117/1.JBO.20.5.051015
History: Received September 1, 2014; Accepted October 30, 2014
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Abstract.  The analysis of the structure-function relationship is extremely important in the study of proteins. The importance of function-related motions of large parts or subglobules of protein molecules stimulates the spectroscopic study in the low-frequency (terahertz) domain. However, only tentative assignments are available and the spectroscopic data are insufficiently discussed in terms of structural changes. This work is aimed at the analysis of regularities of changes in the low-frequency (100 to 600cm1) FTIR and Raman spectra of proteins related to their structural modifications. We study the spectra of two proteins with substantially different structures (albumin and chymotrypsin) and the spectra of samples in which the structures of protein molecules are modified using inhibition, thermal denaturation, and cleavage of disulfide bonds. The results indicate that the low-frequency spectral interval can be used to characterize protein conformations. Correlated variations in the intensities of several low-frequency bands are revealed in the spectra of the modified proteins. The strongest spectral changes are caused by thermal denaturation of proteins, and the effect of cleavage of disulfide bonds is generally weaker. It is demonstrated that the inhibitor binding in the active site causes spectral changes that can be compared to the changes induced by thermal denaturation.

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© 2015 Society of Photo-Optical Instrumentation Engineers

Citation

Nikolay N. Brandt ; Andrey Yu Chikishev ; Anna A. Mankova and Inna K. Sakodynskaya
"Effect of thermal denaturation, inhibition, and cleavage of disulfide bonds on the low-frequency Raman and FTIR spectra of chymotrypsin and albumin", J. Biomed. Opt. 20(5), 051015 (Dec 05, 2014). ; http://dx.doi.org/10.1117/1.JBO.20.5.051015


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