The morphology of decorated amyloid fibers is controlled by the conformation and position of the displayed protein.

Journal article

Self-assembled structures capable of mediating electron transfer are an attractive scientific and technological goal. Therefore, systematic variants of SH3-Cytochrome b(562) fusion proteins were designed to make amyloid fibers displaying heme-b(562) electron transfer complexes. TEM and AFM data show that fiber morphology responds systematically to placement of b(562) within the fusion proteins. UV-vis spectroscopy shows that, for the fusion proteins under test, only half the fiber-borne b(562...

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Authors: Forman, C; Nickson, A; Anthony-Cahill, S; Baldwin, A; Kaggwa, G

• Publication status: Published
• Journal: ACS nano
• Volume: 6
• Issue: 2
• Pages: 1332-1346
• Publication date: 2012-02-01
• DOI: 10.1021/nn204140a
• EISSN: 1936-086X
• ISSN: 1936-0851
• Language: English
• Keywords: Microscopy, Atomic Force; Models, Molecular; Cytochrome b Group; Recombinant Fusion Proteins; Electron Transport; Amyloid; Protein Multimerization; src Homology Domains; Heme