Publication | Open Access
Insights into the Molecular Architecture of a Peptide Nanotube Using FTIR and Solid‐State NMR Spectroscopic Measurements on an Aligned Sample
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Citations
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References
2013
Year
Peptide AaaaaakNatural SciencesPeptide EngineeringPeptide LibraryMolecular ArchitectureConformational StudyPeptide SynthesisPeptide ScienceAligned SampleMolecular BiophysicsAnalytical UltracentrifugationSolution Nmr SpectroscopyMedicineMolecular ModelingIr SpectroscopyBiophysicsBiomolecular EngineeringSolid-state Nmr
Queuing up: Molecular orientation within macroscopically aligned nanotubes of the peptide AAAAAAK can be studied by solid-state NMR and IR spectroscopy. Line shape analysis of the NMR spectra indicates that the peptide N-H bonds are tilted 65-70° relative to the nanotube long axis. Re-evaluation of earlier X-ray fiber diffraction data suggests that the peptide molecules are hydrogen-bonded in a helical arrangement along the nanotube axis.
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