alpha-Synuclein conformations followed by vibrational optical activity. Simulation and understanding of the spectra

Result code in IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61989592%3A15310%2F21%3A73607479" target="_blank" >RIV/61989592:15310/21:73607479 - isvavai.cz</a>

Result on the web

<a href="https://pubs.rsc.org/en/content/articlelanding/2021/CP/D1CP02574K" target="_blank" >https://pubs.rsc.org/en/content/articlelanding/2021/CP/D1CP02574K</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1039/d1cp02574k" target="_blank" >10.1039/d1cp02574k</a>

Result language

angličtina

Original language name

alpha-Synuclein conformations followed by vibrational optical activity. Simulation and understanding of the spectra

Original language description

alpha-Synuclein is a neuronal protein which adopts multiple conformations. These can be conveniently studied by the spectroscopy of vibrational optical activity (VOA). However, the interpretation of VOA spectra based on quantum-chemical simulations is difficult. To overcome the hampering of the computations by the protein size, we used the Cartesian tensor transfer technique to investigate links between the spectral shapes and protein structure. Vibrational circular dichroism (VCD) and Raman optical activity (ROA) spectra of alpha-synuclein in disordered, alpha-helical and beta-sheet (fibril) forms were measured and analyzed on the basis of molecular dynamics and density functional theory computations. For the disordered and alpha-helical conformers, a high fidelity of the simulated spectra with a reasonable computational cost was achieved. Most experimental spectral features could be assigned to the structure. So far unreported ROA marker bands of the secondary structure were found for the lower-frequency and CH stretching vibrations. Fibril VCD spectra were simulated with a rigid periodic model of the geometry and the results are consistent with previous studies based on cryogenic electron microscopy. The fibrils also give a specific ROA signal, but unlike VCD it is currently not fully explicable by the simulations. In connection with the computational modeling the VOA spectroscopy thus appears as an extremely useful tool for monitoring alpha-synuclein and other proteins in solutions.

Czech name

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Czech description

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Type

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

CEP classification

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OECD FORD branch

10403 - Physical chemistry

Project

—

Continuities

I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Publication year

2021

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

23

Issue of the periodical within the volume

31

Country of publishing house

GB - UNITED KINGDOM

Number of pages

11

Pages from-to

16635-16645

UT code for WoS article

000678727500001

EID of the result in the Scopus database

2-s2.0-85112716259