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- W2009046675 abstract "Muscular dystrophies arise with various mutations in dystrophin, implicating this protein in force transmission in normal muscle. With 24 three-helix, spectrin repeats interspersed with proline-rich hinges, dystrophin's large size is an impediment to gene therapy, prompting the construction of mini-dystrophins. Results thus far in dystrophic mice suggest that at least one hinge between repeats is necessary though not sufficient for palliative effect. One such mini-dystrophin is studied here in forced extension at the single molecule level. Δ2331 consists of repeats (R) and hinges (H) H1-R1-2∼H3∼R22-24-H4 linked by native (−) and non-native (∼) sequence. This is compared to its core fragment R2∼H3∼R22 as well as an eight-repeat rod fragment middle (RFM: R8-15). We show by atomic force microscopy that all repeats extend and unfold at forces comparable to those that a few myosin molecules can generate. The hinge regions most often extend and transmit force while limiting tandem repeat unfolding. From 23–42 °C, the dystrophin constructs also appear less temperature-sensitive in unfolding compared to a well-studied βI-spectrin construct. The results thus reveal new modes of dystrophin flexibility that may prove central to functions of both dystrophin and mini-dystrophins." @default.
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- W2009046675 date "2005-09-01" @default.
- W2009046675 modified "2023-10-15" @default.
- W2009046675 title "Molecular Extensibility of Mini-dystrophins and a Dystrophin Rod Construct" @default.
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- W2009046675 doi "https://doi.org/10.1016/j.jmb.2005.07.064" @default.
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