Medical College of Wisconsin
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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

11/03/2015

Pubmed ID

26523295

DOI

10.1039/c5cc05801e

Scopus ID

2-s2.0-84983203520   3 Citations

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.

Author List

Harvey SR, MacPhee CE, Volkman BF, Barran PE

Author

Brian F. Volkman PhD Professor in the Biochemistry department at Medical College of Wisconsin




MESH terms used to index this publication - Major topics in bold

Chemokines, C
Lymphokines
Macromolecular Substances
Microscopy, Electron, Transmission
Peptide Fragments
Polysaccharides
Protein Aggregates
Protein Binding
Protein Structure, Quaternary
Protein Structure, Tertiary
Sialoglycoproteins
jenkins-FCD Prod-444 eb4ebd1a08581aba961d3befd3b851a3c3ec6b46