Abstract
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.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Bacterial Proteins / chemistry*
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Bridged-Ring Compounds / chemistry*
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Imidazoles / chemistry*
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Luminescent Proteins / chemistry*
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Models, Molecular
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Molecular Weight
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Protein Multimerization
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Protein Structure, Secondary
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Recombinant Fusion Proteins / chemistry*
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Scattering, Small Angle
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Solutions
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X-Ray Diffraction
Substances
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Bacterial Proteins
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Bridged-Ring Compounds
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Imidazoles
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Luminescent Proteins
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Recombinant Fusion Proteins
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Solutions
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cucurbit(8)uril
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yellow fluorescent protein, Bacteria