Dustin P. Patterson
University of Texas at Tyler
20 Papers
50 Citations
Dustin P. Patterson is an academic researcher from University of Texas at Tyler. The author has contributed to research in topics: Chemistry & Virus. The author has an hindex of 13, co-authored 18 publications. Previous affiliations of Dustin P. Patterson include Montana State University & Indiana University.
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Papers
Nanoreactors by Programmed Enzyme Encapsulation Inside the Capsid of the Bacteriophage P22
TL;DR: The present study demonstrates incorporation of an enzyme, alcohol dehydrogenase D, with the highest internal loading for an active enzyme by any VLP described thus far, demonstrating that P22 holds potential for synthetic approaches to create nanoreactors, by design, using the power of highly evolved enzymes for chemical transformations.
Encapsulation of an Enzyme Cascade within the Bacteriophage P22 Virus-Like Particle
TL;DR: A biomimetic approach for constructing densely packed and confined multienzyme systems through the co-encapsulation of 2 and 3 enzymes within a virus-like particle that perform a coupled cascade of reactions, creating a synthetic metabolon is described.
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Virus-like particle nanoreactors: programmed encapsulation of the thermostable CelB glycosidase inside the P22 capsid
Dustin P. Patterson,Benjamin Schwarz,Kheireddine El-Boubbou,John van der Oost,Peter E. Prevelige,Trevor Douglas +5 more
TL;DR: The hierarchical bottom-up assembly of bacteriophage P22 virus-like particles (VLPs) that encapsulate the thermostable CelB glycosidase creating catalytically active nanoreactors producing P22 VLPs with a high packaging density of the tetrameric CelB, but without loss of enzyme activity.
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Modular Self-Assembly of Protein Cage Lattices for Multistep Catalysis.
Masaki Uchida,Kimberly McCoy,Masafumi Fukuto,Lin Yang,Hideyuki Yoshimura,Hideyuki Yoshimura,Heini M. Miettinen,Ben LaFrance,Dustin P. Patterson,Benjamin Schwarz,Jonathan A. Karty,Peter E. Prevelige,Byeongdu Lee,Trevor Douglas +13 more
TL;DR: This study demonstrates a significant step toward the bottom-up fabrication of functional superlattice materials using a self-assembly process across multiple length scales and exhibits properties and function that arise from the interaction between individual building blocks.
Rescuing recombinant proteins by sequestration into the P22 VLP
TL;DR: The use of a self-assembling protein cage to sequester and solubilize recombinant proteins which are usually trafficked to insoluble inclusion bodies is reported.
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