Three Conformations of Polyglutamic Acid Monitored by Vibrational Optical Activity
The result's identifiers
Result code in IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61388963%3A_____%2F25%3A00643741" target="_blank" >RIV/61388963:_____/25:00643741 - isvavai.cz</a>
Alternative codes found
RIV/61989592:15310/25:73633300
Result on the web
<a href="https://doi.org/10.1021/acs.analchem.5c05531" target="_blank" >https://doi.org/10.1021/acs.analchem.5c05531</a>
DOI - Digital Object Identifier
<a href="http://dx.doi.org/10.1021/acs.analchem.5c05531" target="_blank" >10.1021/acs.analchem.5c05531</a>
Alternative languages
Result language
angličtina
Original language name
Three Conformations of Polyglutamic Acid Monitored by Vibrational Optical Activity
Original language description
Polyglutamic acid (PGA) is an excellent model system to study peptide and protein folding. Its conformation in solution can be conveniently studied by vibrational optical activity. To better understand the behavior of the molecule in different protonation states and advance the spectroscopic methodology, we obtained infrared (IR), vibrational circular dichroism (VCD), Raman, and Raman optical activity (ROA) spectra of various PGA forms and interpreted them on the basis of molecular dynamics (MD) and density functional theory (DFT) computations. The spectra include the ROA of PGA fibrils, which have been rather unexplored so far. The fibrils provided a distinct ROA pattern, which could be verified by the measurement of both enantiomers. Advancements in the use of vibrational spectroscopy for amyloid fibrils may contribute to the understanding of the biological role of these protein forms, often accompanying neurodegenerative diseases. The computations provided a reliable link between the spectral shapes and molecular geometry, and the simulated spectra reproduced the most important experimental features, although band-to-band simulations of the fibril vibrational optical activity remain challenging. The results nevertheless clearly show that vibrational optical activity combined with spectral simulations appears as a handy tool to study the geometry of proteins, including their aggregates.
Czech name
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Czech description
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Classification
Type
J<sub>imp</sub> - Article in a specialist periodical, which is included in the Web of Science database
CEP classification
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OECD FORD branch
10406 - Analytical chemistry
Result continuities
Project
<a href="/en/project/GA24-10558S" target="_blank" >GA24-10558S: Development of chiral vibrational spectroscopy for solid state systems</a><br>
Continuities
I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace
Others
Publication year
2025
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů
Data specific for result type
Name of the periodical
Analytical Chemistry
ISSN
0003-2700
e-ISSN
1520-6882
Volume of the periodical
97
Issue of the periodical within the volume
50
Country of publishing house
US - UNITED STATES
Number of pages
8
Pages from-to
27913-27920
UT code for WoS article
001638317000001
EID of the result in the Scopus database
2-s2.0-105025223484