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. Author manuscript; available in PMC: 2013 Mar 1.

Published in final edited form as: J Am Soc Mass Spectrom. 2011 Dec 30;23(3):505–519. doi: 10.1007/s13361-011-0309-3

Fig. 6 — Correlation of calculated primary cleavage probability of CBD residues in Molecules A (left) and B (right) with MS trypsin and chymotrypsin (a, apo-; b, calcium-bound) digest results. Colored bars indicate cleavage at t=0 (red), t=10min (green), t=20–30min (purple), t=50min-1hr (blue), or no observed cleavage (gray). Primary cleavage sites determined by MS are indicated by starred (*) residues. ‡Note: Probability values for residues K896, K988, K900 (a, apo-, trypsin) should be significantly higher than all other residues due to high mobility of the N-terminal arm region, yet the values as shown reflect the underestimated crystallographic B-factors used to calculate probability for these residues. See Tables I and II in Supplemental Data for raw data values

Fig. 6 — Correlation of calculated primary cleavage probability of CBD residues in Molecules A (left) and B (right) with MS trypsin and chymotrypsin (a, apo-; b, calcium-bound) digest results. Colored bars indicate cleavage at t=0 (red), t=10min (green), t=20–30min (purple), t=50min-1hr (blue), or no observed cleavage (gray). Primary cleavage sites determined by MS are indicated by starred (*) residues. ‡Note: Probability values for residues K896, K988, K900 (a, apo-, trypsin) should be significantly higher than all other residues due to high mobility of the N-terminal arm region, yet the values as shown reflect the underestimated crystallographic B-factors used to calculate probability for these residues. See Tables I and II in Supplemental Data for raw data values