The 3D Solution Structure of Thurincin H, a Bacteriocin with Four Sulfur to α-Carbon Crosslinks

The 3D Solution Structure of Thurincin H, a Bacteriocin with Four Sulfur to α-Carbon Crosslinks

Problem solved: Thurincin H is an antimicrobial peptide with suspected post‐translational modifications. MS/MS sequencing identified the residues that were modified, and NMR spectroscopic studies in solution led to the 3D structure of thurincin H, which features four SCα thioether crosslinks (yello...

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Veröffentlicht in:Angewandte Chemie International Edition 2011-09, Vol.50 (37), p.8718-8721
Hauptverfasser: Sit, Clarissa S., van Belkum, Marco J., McKay, Ryan T., Worobo, Randy W., Vederas, John C.
Format: Artikel
Sprache:eng
Schlagworte:
bacteriocins
Bacteriocins - chemistry
Bacteriocins - isolation & purification
Carbon - chemistry
mass spectrometry
Models, Molecular
Molecular Conformation
NMR spectroscopy
peptides
Solutions
structure elucidation
Sulfur - chemistry
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Zusammenfassung:Problem solved: Thurincin H is an antimicrobial peptide with suspected post‐translational modifications. MS/MS sequencing identified the residues that were modified, and NMR spectroscopic studies in solution led to the 3D structure of thurincin H, which features four SCα thioether crosslinks (yellow in schematic representation). This structure may be representative of several other bacteriocins with identical masses.
ISSN:1433-7851
1521-3773
DOI:10.1002/anie.201102527