Enzyme Nanorings
Creators
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1.
University of Washington
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2.
University of Minnesota
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.
Additional Information
© 2008 American Chemical Society. Received 14 September 2008. Accepted 22 November 2008. Published online 9 December 2008. Published in issue 23 December 2008. We thank Dr. Terry W. Steele for his assistance with the SLS experiments, and Dr. R. A. Siegel for the use of the SLS instrument. We wish to thank the University of Minnesota Nanobiotechnology Initiative (C.R.W.), NIH-NCI (CA120116, C.R.W.), the Leukemia Research Foundation, and NSF-MRSEC (C.S. and M.S.) for partial support of this study (DMR-0520567).Attached Files
Accepted Version - nihms91468.pdf
Supplemental Material - nn800577h_si_001.pdf
Files
nihms91468.pdf
Additional details
Identifiers
- PMCID
- PMC2682639
- Eprint ID
- 114034
- Resolver ID
- CaltechAUTHORS:20220323-565456000
Funding
- University of Minnesota
- NIH
- CA120116
- Leukemia Research Foundation
- NSF
- DMR-0520567
Dates
- Created
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2022-03-25Created from EPrint's datestamp field
- Updated
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2022-03-25Created from EPrint's last_modified field