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Stable single α-helices are constant force springs in proteins.

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Figure

FIGURE 1. Intrahelical ionic interactions and circular dichroism of the pre-values fromthe measured MRE values at 222 nm to be 67%.the SAH domain compared with that for a known coiled coil (M2CC)
FIGURE 2. I275-SAH constructs and their circular dichroism spectra. A shows the three constructs used in these experiments: I275, I275SAH1 (which containsa single myosin-10 SAH domain (residues 813–909)), and I275SAH2 (which contains two myosin-10 SAH doma
FIGURE 4. Analysis of single molecule force spectroscopy results for I27I27 unfolding event for each of the three constructs
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