Insight into vibrational circular dichroism of proteins by density functional modeling

Result code in IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61388963%3A_____%2F18%3A00489618" target="_blank" >RIV/61388963:_____/18:00489618 - isvavai.cz</a>

Alternative codes found

RIV/61989592:15310/18:73587163

Result on the web

<a href="https://pubs.rsc.org/en/content/articlehtml/2018/cp/c7cp08016f" target="_blank" >https://pubs.rsc.org/en/content/articlehtml/2018/cp/c7cp08016f</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1039/c7cp08016f" target="_blank" >10.1039/c7cp08016f</a>

Result language

angličtina

Original language name

Insight into vibrational circular dichroism of proteins by density functional modeling

Original language description

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.

Czech name

—

Czech description

—

Type

J_imp - Article in a specialist periodical, which is included in the Web of Science database

CEP classification

—

OECD FORD branch

10403 - Physical chemistry

Project

Result was created during the realization of more than one project. More information in the Projects tab.

Continuities

P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)

Publication year

2018

Confidentiality

S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Name of the periodical

Physical Chemistry Chemical Physics

ISSN

1463-9076

e-ISSN

—

Volume of the periodical

20

Issue of the periodical within the volume

7

Country of publishing house

GB - UNITED KINGDOM

Number of pages

10

Pages from-to

4926-4935

UT code for WoS article

000425107800032

EID of the result in the Scopus database

2-s2.0-85042144980