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. Author manuscript; available in PMC: 2019 Sep 1.
Published in final edited form as: J Struct Biol. 2018 May 11;203(3):255–262. doi: 10.1016/j.jsb.2018.05.003

Figure 3.

Figure 3.

Trypsin digestion of the recombinant bacterial protein with Gly to Ala, Gly to Ser and Gly to Val mutations at positions 502, 505, 508 and 511 in the 6-triplet insertion. SDS- PAGE of all recombinant collagens after trypsin digestion for time t=0, 2, and 15 min at 20°C. G502S, G502V, G505V and G511V showed various levels of trypsin susceptibility. Mutants completely degraded within 15 min were highlighted with red; mutants susceptible to trypsin but incompletely degraded within 15 min were highlighted with orange. Lane M, Novex® Sharp protein standard (Invitrogen); collagen monomer chains run slower than expected, as reported previously; molecular mass indicated in kDa.