Modeling the structure of crystalline alamethicin and its NMR chemical shift tensors
The result's identifiers
Result code in IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61389013%3A_____%2F21%3A00546945" target="_blank" >RIV/61389013:_____/21:00546945 - isvavai.cz</a>
Result on the web
<a href="https://www.mdpi.com/2079-6382/10/10/1265" target="_blank" >https://www.mdpi.com/2079-6382/10/10/1265</a>
DOI - Digital Object Identifier
<a href="http://dx.doi.org/10.3390/antibiotics10101265" target="_blank" >10.3390/antibiotics10101265</a>
Alternative languages
Result language
angličtina
Original language name
Modeling the structure of crystalline alamethicin and its NMR chemical shift tensors
Original language description
Alamethicin (ALM) is an antimicrobial peptide that is frequently employed in studies of the mechanism of action of pore-forming molecules. Advanced techniques of solid-state NMR spectroscopy (SSNMR) are important in these studies, as they are capable of describing the alignment of helical peptides, such as ALM, in lipid bilayers. Here, it is demonstrated how an analysis of the SSNMR measurements can benefit from fully periodic calculations, which employ the plane-wave density-functional theory (PW DFT) of the solid-phase geometry and related spectral parameters of ALM. The PW DFT calculations are used to obtain the structure of desolvated crystalline ALM and predict the NMR chemical shift tensors (CSTs) of its nuclei. A variation in the CSTs of the amidic nitrogens and carbonyl carbons along the ALM backbone is evaluated and included in simulations of the orientation-dependent anisotropic 15N and 13C chemical shift components. In this way, the influence of the site-specific structural effects on the experimentally determined orientation of ALM is shown in models of cell membranes.
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
10403 - Physical chemistry
Result continuities
Project
<a href="/en/project/LTAUSA18011" target="_blank" >LTAUSA18011: Ab Initio Investigation of Polymorphism of Active Pharmaceutical Ingredients Supported by State of the Art NMR Crystallographic and Calorimetric Experiments.</a><br>
Continuities
I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace
Others
Publication year
2021
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů
Data specific for result type
Name of the periodical
Antibiotics (Basel)
ISSN
2079-6382
e-ISSN
2079-6382
Volume of the periodical
10
Issue of the periodical within the volume
10
Country of publishing house
CH - SWITZERLAND
Number of pages
12
Pages from-to
1265
UT code for WoS article
000715441600001
EID of the result in the Scopus database
2-s2.0-85118200430