| Literature DB >> 18710226 |
Karen A McAllister1, Hongling Zou, Frank V Cochran, Gretchen M Bender, Alessandro Senes, H Christopher Fry, Vikas Nanda, Patricia A Keenan, James D Lear, Jeffery G Saven, Michael J Therien, J Kent Blasie, William F DeGrado.
Abstract
We have developed a computational design strategy based on the alpha-helical coiled-coil to generate modular peptide motifs capable of assembling into metalloporphyrin arrays of varying lengths. The current study highlights the extension of a two-metalloporphyrin array to a four-metalloporphyrin array through the incorporation of a coiled-coil repeat unit. Molecular dynamics simulations demonstrate that the initial design evolves rapidly to a stable structure with a small rmsd compared to the original model. Biophysical characterization reveals elongated proteins of the desired length, correct cofactor stoichiometry, and cofactor specificity. The successful extension of the two-porphyrin array demonstrates how this methodology serves as a foundation to create linear assemblies of organized electrically and optically responsive cofactors.Entities:
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Year: 2008 PMID: 18710226 PMCID: PMC3663296 DOI: 10.1021/ja800697g
Source DB: PubMed Journal: J Am Chem Soc ISSN: 0002-7863 Impact factor: 15.419