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The design of new proteins and enzymes remains one of the great challenges in biochemistry and tests our fundamental understanding of both the nature of protein as a material and the principles of enzymatic catalysis. Unlocking the exceptionally diverse and powerful array of chemistries exhibited by natural enzymes promises routes to new drugs, therapies and green industrial processes.
Most approaches to this end have focused on modifying natural enzymes to impart new or altered catalytic function. The problems that often hinder the re-engineering of naturally evolved proteins and enzymes are due to the layers of complexity that nature incorporates through natural selection into a protein’s complex 3D structure.
Simplified manmade protein scaffolds offer a means to avoid such complexity, learn the principles guiding functional protein assembly and render the modular assembly of enzymatic function a tangible reality. This approach is illustrated through the assembly of artificial oxygen binding proteins that reproduce the function of natural proteins such as myoglobin in simple heme-binding 4-helix bundles untouched by natural selection. The tractable design process that we employ resolves the roles of individual amino acids with their function and opens the door to the powerful oxygenic catalysis common to heme-containing enzymes.
In my laboratory, we use this simple protein design approach to construct artificial oxidoreductase enzymes that integrate functional elements common to natural redox enzymes - e.g. electron/proton transfer, ligand/substrate binding and light harvesting - in a discrete manmade protein that is wholly fabricated within a living organism.
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Creating and comprehending the circuitry of life: precise biomolecular design of multi-centre redox enzymes for a synthetic metabolism
1/08/22 → 31/07/27
Project: Research, Parent
1/11/18 → 31/03/22
Hutchins, G. H., Noble, C. E. M., Bunzel, H. A., Williams, C., Dubiel, P., Yadav, S. K. N., Molinaro, P. M., Barringer, R., Blackburn, H., Hardy, B. J., Parnell, A. E., Landau, C., Race, P. R., Oliver, T. A. A., Koder, R. L., Crump, M. P., Schaffitzel, C., Oliveira, A. S. F., Mulholland, A. J. & Anderson, J. L. R., 24 Jul 2023, In: Proceedings of the National Academy of Sciences of the United States of America. 120, 31, e2306046120.
Research output: Contribution to journal › Article (Academic Journal) › peer-reviewOpen Access1 Citation (Scopus)
Antibodies generated<i>in vitro</i>and<i>in vivo</i>elucidate design of a thermostable ADDomer COVID-19 nasal nanoparticle vaccineBuzas, D., Bunzel, H. A., Staufer, O., Milodowski, E., Edmonds, G., Bufton, J., Vidana, B., Yadav, S., Gupta, K., Fletcher, C., Williamson, M. K., Harrison, A., Borucu, U., Capin, J., Francis, O., Balchin, G., Hall, S., Vega, M. V., Fabien, DURBESSON., Vincentelli, R., & 16 others, 17 Mar 2023
Research output: Other contribution
Hardy, B. J., Hermosilla, A. M., Chinthapalli, D. K., Robinson, C. V., Anderson, J. L. R. & Curnow, P., 18 Apr 2023, In: Proceedings of the National Academy of Sciences of the United States of America. 120, 16, e2300137120.
Research output: Contribution to journal › Article (Academic Journal) › peer-reviewOpen Access
Anderson, J. L. R. (Creator), Watkins, D. (Creator), Jenkins, J. (Creator), Coutable, A. (Creator), Frank, B. (Creator), Bunzel, H. (Creator), Neary, T. E. (Creator), Dubiel, P. (Creator), Noble, C. (Creator), Hutchins, G. (Creator), Stenner, R. A. (Creator) & Bungay, E. (Creator), University of Bristol, 15 Feb 2023
Bunzel, A. (Creator), Mulholland, A. J. (Creator), Anderson, J. L. R. (Contributor), Hilvert, D. (Contributor), Arcus, V. L. (Contributor) & Van der Kamp, M. W. (Contributor), University of Bristol, 18 Jun 2021
J L R Anderson (Recipient)1 Oct 2009 → 1 Oct 2014
Activity: Other activity types › Fellowship awarded competitively