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Barry D. Bruce

Researcher at University of Tennessee

Publications -  131
Citations -  7452

Barry D. Bruce is an academic researcher from University of Tennessee. The author has contributed to research in topics: Photosystem I & Transit Peptide. The author has an hindex of 45, co-authored 123 publications receiving 6671 citations. Previous affiliations of Barry D. Bruce include Massachusetts Institute of Technology & University of Massachusetts Amherst.

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Liposomal Nanocapsules in Food Science and Agriculture

TL;DR: Key physicochemical properties of liposomes are introduced and competing methods for liposome production are reviewed and a detailed up-to-date summary of the emerging usage ofliposomes in the food industry as delivery vehicles of nutrients, nutraceuticals, food additives, and food antimicrobials is provided.
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Structural and functional changes in ultrasonicated bovine serum albumin solutions.

TL;DR: It is hypothesized that mechanical, thermal and chemical effects of ultrasonication resulted in structural changes in BSA that altered the functional properties of the macromolecule which may be attributed to the formation of an ultrasonically induced state that differs from a thermally, mechanically or solvent induced state.
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Biofuel production: Challenges and opportunities

TL;DR: Future research endeavors in biofuels production should be placed on the search of novel biofuel production species, optimization and improvement of culture conditions, genetic engineering of biofuel-producing species, and effective techniques for mass cultivation of microorganisms.
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Integration of Photosynthetic Protein Molecular Complexes in Solid-State Electronic Devices

TL;DR: In this paper, the integration of electrically active photosynthetic protein−molecular complexes in solid-state devices was demonstrated, achieving photodetectors and photovoltaic cells with internal quantum efficiencies of approximately 12%.
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Chloroplast transit peptides: structure, function and evolution

TL;DR: The genomic organization of transit peptides suggests that these domains might have originated from distinct exons, which were shuffled and streamlined throughout evolution to yield a modern, multifunctional transit peptide.