Počet záznamů: 1
Insight into vibrational circular dichroism of proteins by density functional modeling
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SYSNO ASEP 0489618 Druh ASEP J - Článek v odborném periodiku Zařazení RIV J - Článek v odborném periodiku Poddruh J Článek ve WOS Název Insight into vibrational circular dichroism of proteins by density functional modeling Tvůrce(i) Kessler, Jiří (UOCHB-X) RID, ORCID
Andrushchenko, Valery (UOCHB-X) RID, ORCID
Kapitán, J. (CZ)
Bouř, Petr (UOCHB-X) RID, ORCIDZdroj.dok. Physical Chemistry Chemical Physics. - : Royal Society of Chemistry - ISSN 1463-9076
Roč. 20, č. 7 (2018), s. 4926-4935Poč.str. 10 s. Jazyk dok. eng - angličtina Země vyd. GB - Velká Británie Klíč. slova Raman optical activity ; molecular property tensors ; coupled oscillator model Vědní obor RIV CF - Fyzikální chemie a teoretická chemie Obor OECD Physical chemistry CEP LTC17012 GA MŠMT - Ministerstvo školství, mládeže a tělovýchovy GA16-05935S GA ČR - Grantová agentura ČR GA16-04902S GA ČR - Grantová agentura ČR EF16_019/0000729 GA MŠMT - Ministerstvo školství, mládeže a tělovýchovy Institucionální podpora UOCHB-X - RVO:61388963 UT WOS 000425107800032 EID SCOPUS 85042144980 DOI 10.1039/c7cp08016f Anotace 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. Pracoviště Ústav organické chemie a biochemie Kontakt asep@uochb.cas.cz ; Kateřina Šperková, Tel.: 232 002 584 ; Viktorie Chládková, Tel.: 232 002 434 Rok sběru 2019 Elektronická adresa https://pubs.rsc.org/en/content/articlehtml/2018/cp/c7cp08016f
Počet záznamů: 1