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Insight into vibrational circular dichroism of proteins by density functional modeling
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SYSNO ASEP 0489618 Document Type J - Journal Article R&D Document Type Journal Article Subsidiary J Článek ve WOS Title Insight into vibrational circular dichroism of proteins by density functional modeling Author(s) Kessler, Jiří (UOCHB-X) RID, ORCID
Andrushchenko, Valery (UOCHB-X) RID, ORCID
Kapitán, J. (CZ)
Bouř, Petr (UOCHB-X) RID, ORCIDSource Title Physical Chemistry Chemical Physics. - : Royal Society of Chemistry - ISSN 1463-9076
Roč. 20, č. 7 (2018), s. 4926-4935Number of pages 10 s. Language eng - English Country GB - United Kingdom Keywords Raman optical activity ; molecular property tensors ; coupled oscillator model Subject RIV CF - Physical ; Theoretical Chemistry OECD category Physical chemistry R&D Projects LTC17012 GA MŠMT - Ministry of Education, Youth and Sports (MEYS) GA16-05935S GA ČR - Czech Science Foundation (CSF) GA16-04902S GA ČR - Czech Science Foundation (CSF) EF16_019/0000729 GA MŠMT - Ministry of Education, Youth and Sports (MEYS) Institutional support UOCHB-X - RVO:61388963 UT WOS 000425107800032 EID SCOPUS 85042144980 DOI 10.1039/c7cp08016f Annotation Vibrational circular dichroism (VCD) spectroscopy is an excellent method to determine the secondary structure of proteins in solution. Comparison of experimental spectra with quantum-chemical simulations represents a convenient and objective way to extract information on the structure. This has been difficult for such large molecules where approximate theoretical models have to be used. In the present study we applied the Cartesian-coordinate based tensor transfer (CCT) making it possible to extend the density functional theory (DFT) and model spectral intensities of large globular proteins nearly at quantum-chemical precision. Indeed, comparison with experiment provided a better understanding of the dependence of VCD spectral shapes on the geometry, their sensitivity to fine structural details and interactions with the environment. On a model set of globular proteins the simulated spectra correlated well with experimental data and revealed which structural information can (and cannot) be obtained from this kind of spectroscopy. Although the VCD technique has been regarded as being rather insensitive to side-chain variations, we found that the spectra of human and hen lysozyme differing by a few amino acids only are quite distinct. This has been explained by long-distance coupling of the amide vibrations. Likewise, the modeling reproduced some spectral changes caused by protein deuteration even when the protein structure was conserved. Workplace Institute of Organic Chemistry and Biochemistry Contact asep@uochb.cas.cz ; Kateřina Šperková, Tel.: 232 002 584 ; Jana Procházková, Tel.: 220 183 418 Year of Publishing 2019 Electronic address https://pubs.rsc.org/en/content/articlehtml/2018/cp/c7cp08016f
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