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- W1980419942 abstract "The de novo design of membrane proteins remains difficult despite recent advances in understanding the factors that drive membrane protein folding and association. We have designed a membrane protein PRIME (PoRphyrins In MEmbrane) that positions two non-natural iron diphenylporphyrins (FeIIIDPP’s) sufficiently close to provide a multicentered pathway for transmembrane electron transfer. Computational methods previously used for the design of multiporphyrin water-soluble helical proteins were extended to this membrane target. Four helices were arranged in a D2-symmetrical bundle to bind two Fe(II/III) diphenylporphyrins in a bis-His geometry further stabilized by second-shell hydrogen bonds. UV−vis absorbance, CD spectroscopy, analytical ultracentrifugation, redox potentiometry, and EPR demonstrate that PRIME binds the cofactor with high affinity and specificity in the expected geometry." @default.
- W1980419942 created "2016-06-24" @default.
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- W1980419942 date "2010-10-14" @default.
- W1980419942 modified "2023-10-18" @default.
- W1980419942 title "De Novo Design and Molecular Assembly of a Transmembrane Diporphyrin-Binding Protein Complex" @default.
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- W1980419942 doi "https://doi.org/10.1021/ja107487b" @default.
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