ArticleJournal of biomolecular NMR2009
Analysis of the amide (15)N chemical shift tensor of the C(alpha) tetrasubstituted constituent of membrane-active peptaibols, the alpha-aminoisobutyric acid residue, compared to those of di- and tri-substituted proteinogenic amino acid residues.
Article in Journal of biomolecular NMR, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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17 citing papers in PubMed, 36 citations in OpenAlex.
- Membrane Topology and Oligomerization of Peptaibols by Solid-State NMR Spectroscopy.Journal of peptide science : an official publication of the European Peptide Society · 2026Review
- A kink in DWORF helical structure controls the activation of the sarcoplasmic reticulum CaStructure (London, England : 1993) · 2022Article
- Modeling the Structure of Crystalline Alamethicin and Its NMR Chemical Shift Tensors.Antibiotics (Basel, Switzerland) · 2021Article
- Article
- Structure, membrane topology and influence of cholesterol of the membrane proximal region: transmembrane helical anchor sequence of gp41 from HIV.Scientific reports · 2020Article
- Monitoring the Site-Specific Solid-State NMR Data in Oligopeptides.International journal of molecular sciences · 2020Article
- Review
- A theoretical assessment of structure determination of multi-span membrane proteins by oriented sample solid-state NMR spectroscopy.Australian journal of chemistry · 2020Article
- Solid-State NMR Investigations of the MHC II Transmembrane Domains: Topological Equilibria and Lipid Interactions.The Journal of membrane biology · 2019Article
- Structure, Topology, and Dynamics of Membrane-Inserted Polypeptides and Lipids by Solid-State NMR Spectroscopy: Investigations of the Transmembrane Domains of the DQ Beta-1 Subunit of the MHC II Receptor and of the COP I Protein p24.Frontiers in molecular biosciences · 2019Article
- Supramolecular Organization of Apolipoprotein-A-I-Derived Peptides within Disc-like Arrangements.Biophysical journal · 2018Article
- Structural Characterization of the Amyloid Precursor Protein Transmembrane Domain and Its γ-Cleavage Site.ACS omega · 2017Article
- Probing the Huntingtin 1-17 membrane anchor on a phospholipid bilayer by using all-atom simulations.Biophysical journal · 2015Article
- (14)N overtone NMR under MAS: signal enhancement using symmetry-based sequences and novel simulation strategies.Physical chemistry chemical physics : PCCP · 2015Article
- Membrane interactions of phylloseptin-1, -2, and -3 peptides by oriented solid-state NMR spectroscopy.Biophysical journal · 2014Article
- Probing the transmembrane structure and dynamics of microsomal NADPH-cytochrome P450 oxidoreductase by solid-state NMR.Biophysical journal · 2014Article
- Structure and topology of the huntingtin 1-17 membrane anchor by a combined solution and solid-state NMR approach.Biophysical journal · 2013Article
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Authors and funding
4 authors at 3 institutions in 2 countries.
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No grant is acknowledged in the PubMed record.
Abstract
In protein NMR spectroscopy the chemical shift provides important information for the assignment of residues and a first structural evaluation of dihedral angles. Furthermore, angular restraints are obtained from oriented samples by solution and solid-state NMR spectroscopic approaches. Whereas the anisotropy of chemical shifts, quadrupolar couplings and dipolar interactions have been used to determine the structure, dynamics and topology of oriented membrane polypeptides using solid-state NMR spectroscopy similar concepts have been introduced to solution NMR through the measurements of residual dipolar couplings. The analysis of (15)N chemical shift spectra depends on the accuracy of the chemical shift tensors. When investigating alamethicin and other peptaibols, i.e. polypeptides rich in alpha-aminoisobutyric acid (Aib), the (15)N chemical shift tensor of this C(alpha)-tetrasubstituted amino acid exhibits pronounced differences when compared to glycine, alanine and other proteinogenic residues. Here we present an experimental investigation on the (15)N amide Aib tensor of N-acetyl-Aib-OH and for the Aib residues within peptaibols. Furthermore, a statistical analysis of the tensors published for di- (glycine) and tri-substituted residues has been performed, where for the first time the published data sets are compiled using a common reference. The size of the isotropic chemical shift and main tensor elements follows the order di- < tri- < tetra-substituted amino acids. A (15)N chemical shift-(1)H-(15)N dipolar coupling correlation NMR spectrum of alamethicin is used to evaluate the consequences of variations in the main tensor elements for the structural analysis of this membrane peptide.
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