Elementary tetrahelical protein design for diverse oxidoreductase functions.
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ABSTRACT: Emulating functions of natural enzymes in man-made constructs has proven challenging. Here we describe a man-made protein platform that reproduces many of the diverse functions of natural oxidoreductases without importing the complex and obscure interactions common to natural proteins. Our design is founded on an elementary, structurally stable 4-α-helix protein monomer with a minimalist interior malleable enough to accommodate various light- and redox-active cofactors and with an exterior tolerating extensive charge patterning for modulation of redox cofactor potentials and environmental interactions. Despite its modest size, the construct offers several independent domains for functional engineering that targets diverse natural activities, including dioxygen binding and superoxide and pe
SUBMITTER: Farid TA
PROVIDER: S-EPMC4034760 | biostudies-literature | 2013 Dec
REPOSITORIES: biostudies-literature
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