z-logo
Premium
The 3D Solution Structure of Thurincin H, a Bacteriocin with Four Sulfur to α‐Carbon Crosslinks
Author(s) -
Sit Clarissa S.,
van Belkum Marco J.,
McKay Ryan T.,
Worobo Randy W.,
Vederas John C.
Publication year - 2011
Publication title -
angewandte chemie international edition
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.831
H-Index - 550
eISSN - 1521-3773
pISSN - 1433-7851
DOI - 10.1002/anie.201102527
Subject(s) - bacteriocin , thioether , chemistry , sulfur , schematic , peptide , combinatorial chemistry , stereochemistry , antimicrobial , organic chemistry , biochemistry , electronic engineering , engineering
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 SC α thioether crosslinks (yellow in schematic representation). This structure may be representative of several other bacteriocins with identical masses.

This content is not available in your region!

Continue researching here.

Having issues? You can contact us here