The association and aggregation of the metamorphic chemokine lymphotactin with fondaparinux: from nm molecular complexes to μm molecular assemblies. Chem Commun (Camb) 2016 Jan 07;52(2):394-7
Date
11/03/2015Pubmed ID
26523295DOI
10.1039/c5cc05801eScopus ID
2-s2.0-84983203520 (requires institutional sign-in at Scopus site) 4 CitationsAbstract
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.
Author List
Harvey SR, MacPhee CE, Volkman BF, Barran PEAuthor
Brian F. Volkman PhD Professor in the Biochemistry department at Medical College of WisconsinMESH terms used to index this publication - Major topics in bold
Chemokines, CLymphokines
Macromolecular Substances
Microscopy, Electron, Transmission
Peptide Fragments
Polysaccharides
Protein Aggregates
Protein Binding
Protein Structure, Quaternary
Protein Structure, Tertiary
Sialoglycoproteins
