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

Sit Clarissa S. | Zendy; van Belkum Marco J. | Zendy; McKay Ryan T. | Zendy; Worobo Randy W. | Zendy; Vederas John C. | Zendy

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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.

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