dc.contributor.authorMahajan, Mukesh
dc.contributor.authorBhattacharjya, Surajit
dc.date.accessioned2014-09-08T08:05:08Z
dc.date.available2014-09-08T08:05:08Z
dc.date.copyright2014en_US
dc.date.issued2014
dc.identifier.citationMahajan, M., & Bhattacharjya, S. (2014). Designed di-heme binding helical transmembrane protein. ChemBioChem, 15(9), 1257-1262.en_US
dc.identifier.issn1439-4227en_US
dc.identifier.urihttp://hdl.handle.net/10220/20460
dc.description.abstractDe novo designing of functional membrane proteins is fundamental in terms of understanding the structure, folding, and stability of membrane proteins. In this work, we report the design and characterization of a transmembrane protein, termed HETPRO (HEme-binding Transmembrane PROtein), that binds two molecules of heme in a membrane and catalyzes oxidation/reduction reactions. The primary structure of HETPRO has been optimized in a guided fashion, from an antimicrobial peptide, for transmembrane orientation, defined 3D structure, and functions. HETPRO assembles into a tetrameric form, from an apo dimeric helical structure, in complex with cofactor in detergent micelles. The NMR structure of the apo HETPRO in micelles reveals an antiparallel helical dimer that inserts into the nonpolar core of detergent micelles. The well-defined structure of HETPRO and its ability to bind to heme moieties could be utilized to develop a functional membrane protein mimic for electron transport and photosystems.en_US
dc.language.isoenen_US
dc.relation.ispartofseriesChemBioChemen_US
dc.rights© 2014 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim.en_US
dc.subjectDRNTU::Science::Biological sciences
dc.titleDesigned di-heme binding helical transmembrane proteinen_US
dc.typeJournal Article
dc.contributor.schoolSchool of Biological Sciencesen_US
dc.identifier.doihttp://dx.doi.org/10.1002/cbic.201402142


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