ArticleAntibiotics (Basel, Switzerland)2021
Modeling the Structure of Crystalline Alamethicin and Its NMR Chemical Shift Tensors.
Article in Antibiotics (Basel, Switzerland), 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.
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The trial behind it
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Who cites it
2 citing papers in PubMed.
- The conformational properties of alamethicin in ethanol studied by NMR.European biophysics journal : EBJ · 2024Article
- Morphology Observation of Two-Dimensional Monolayers of Model Proteins on Water Surface as Revealed by Dropping Method.Bioengineering (Basel, Switzerland) · 2024Article
Corrections and comments
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Authors and funding
2 authors.
Funding
Abstract
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
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