Journal
JOURNAL OF BIOMOLECULAR NMR
Volume 45, Issue 4, Pages 373-387Publisher
SPRINGER
DOI: 10.1007/s10858-009-9380-5
Keywords
Oriented membranes; Oriented bicelles; Chemical shift anisotropy; Oriented lipid bilayer; alpha-Helix; 3(10) Helix; Membrane protein structure determination; Topology; Angular restraints; Tilt and rotational pitch angle
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Funding
- Netherlands Organization of Scientific Research in collaboration with the Russian Foundation of Basic Research [NWO 047.017.034]
- Agence Nationale pour la Recherche
- RMN Grand-Est Network of the French Ministry of Research
- Vaincre la Mucoviscidose [TG0602]
- French government fellowship program (BGF)
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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 N-15 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 N-15 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 N-15 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 N-15 chemical shift-H-1-N-15 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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