Proteolytic enzymes as probes for the triple-helical conformation of procollagen
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Mechanics and structural stability of the collagen triple helix
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2018, Journal of Structural BiologyCitation Excerpt :The DSC melting profiles for G502A, G502S and G502V mutants also exhibited a second lower-stability thermal transition, consistent with the CD results (Fig. S1). The tightly packed triple helix confers resistance to general proteases (Bruckner and Prockop, 1981; Yu et al., 2014), and the recombinant constructs with Gly missense mutants were treated with trypsin to assess disruption of the native triple helix. After a 15-min digestion at 20 °C, the control protein VCL-Int remained resistant to trypsin digestion, as demonstrated by its intact size on SDS-PAGE (Fig. S2A).
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