Enzyme nanorings.
basic_science · Level V
Where this comes from
- Record sourced from PubMed, PMID 19206287.
- Also identified by DOI 10.1021/nn800577h and PMC identifier 2682639.
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Abstract
We have demonstrated that nanostructures, and in particular nanorings incorporating a homodimeric enzyme, can be prepared by chemically induced self-assembly of dihydrofolate reductase (DHFR)-histidine triad nucleotide binding 1 (Hint1) fusion proteins. The dimensions of the nanorings were found by static light scattering and atomic force microscopy studies to be dependent on the length and composition of the peptide linking the fusion proteins, ranging in size from 10 to 70 nm in diameter and 64 to 740 kDa. The catalytic efficiency of the nanorings was found to be dependent on ring size, thus suggesting that the arrangement of supermolecular assemblies of enzymes may be used to control their catalytic parameters.
Medical subject headings
- Nanostructures
- Nerve Tissue Proteins
- Tetrahydrofolate Dehydrogenase