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. Author manuscript; available in PMC: 2021 Jan 17.
Published in final edited form as: J Mol Biol. 2019 Oct 17;432(2):305–323. doi: 10.1016/j.jmb.2019.09.022

Figure 4:

Figure 4:

LTMS correlations between trypsinolysis rates (hr−1) of wild-type (x-coordinates) and mutant A1, A1A2A3, and multimeric VWF constructs (y-coordinates). A) Initial rates of wild-type, P1337L, G1324S and for RCAM A1 relative to wild-type A1. B) Initial rates of the A1 domain within the wild-type, P1337L, F1369I, and V1314D A1A2A3 tridomain relative to wild-type A1A2A3. C) Initial rates of A2 and A3 domains within the wild-type, P1337L, F1369I, and V1314D A1A2A3 tridomain relative to wild-type A1A2A3. D) Initial rates of the A1 domain within the wild-type, P1337L, S1285F, and V1316M VWF relative to the wild-type VWF. E) Initial rates of all other domains outside of the A1A2A3 domain region of VWF in wild-type, P1337L, S1285F, and V1316M VWF relative to the wild-type VWF. F) Control: Initial rates of the wild-type A1, A1A2A3, and VWF constructs relative to wild-type VWF. Panels A-F) Trypsinolysis rates for all data points for every construct are available in the LTMS Supporting Information. Lines represent linear fits with a zero intercept. Linear fits and rates are translated to Log:Log scale. Rates above wild-type indicate faster proteolysis. Those below wild-type represent a slower cleavage of the protein. Error bars on each datapoint represent fitting errors of the initial slope of tryptic peptide peak volume with respect to time (see LTMS Supporting Information Figures S3S10).