The association and aggregation of the metamorphic chemokine lymphotactin with fondaparinux: from nm molecular complexes to μm molecular assemblies. Issue 2 (2nd November 2015)

• Record Type: Journal Article
• Authors: Harvey, Sophie R.; MacPhee, Cait E.; Volkman, Brian F.; Barran, Perdita E.
• Is Part Of: Chemical communications. Volume 52:Issue 2(2016)
• Page Start: 394
• Page End: 397
• Publication Date: 2015-11-02
• Subjects: Chemistry -- Periodicals; 540
• DOI: 10.1039/c5cc05801e
• Languages: English
• ISSNs: 1359-7345

Abstract

Abstract : Transmission electron microscopy and drift tube ion mobility-mass spectrometry are used to study the assemblies formed by the metamorphic chemokine lymphotactin in the presence of a model glycosaminoglycan. Abstract : Transmission electron microscopy, mass spectrometry, and drift tube ion mobility-mass spectrometry are used to study the assemblies formed by the metamorphic chemokine lymphotactin in the presence of a model pentameric glycosaminoglycan, fondaparinux. This combination of techniques delineates significant differences in the complexes observed for two forms of the full length protein as well as a truncated form, without the intrinsically disordered C-terminal tail, over a length scale from few nm to μm assemblies.