Solution structure of a cucurbit[8]uril induced compact supramolecular protein dimer

Supramolecular assembly of a beta-barrel protein via cucurbit[8]uril results in compact z-shaped protein dimers. SAXS data reveal the formation of a well ordered protein dimer, notwithstanding being connected by a reversible and flexible peptide linker, and highlight the supramolecular induced inter...

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Veröffentlicht in:	Organic & biomolecular chemistry 2014-12, Vol.12 (46), p.9341-9344
Hauptverfasser:	Dang, Dung T, Bosmans, Ralph P G, Moitzi, Christian, Voets, Ilja K, Brunsveld, Luc
Format:	Artikel
Sprache:	eng
Schlagworte:	Bacterial Proteins - chemistry Bridged-Ring Compounds - chemistry Imidazoles - chemistry Luminescent Proteins - chemistry Models, Molecular Molecular Weight Protein Multimerization Protein Structure, Secondary Recombinant Fusion Proteins - chemistry Scattering, Small Angle Solutions X-Ray Diffraction
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Zusammenfassung:	Supramolecular assembly of a beta-barrel protein via cucurbit[8]uril results in compact z-shaped protein dimers. SAXS data reveal the formation of a well ordered protein dimer, notwithstanding being connected by a reversible and flexible peptide linker, and highlight the supramolecular induced interplay of the proteins, analogous to covalently linked proteins.
ISSN:	1477-0520 1477-0539
DOI:	10.1039/c4ob01729c