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. 2017 Jan 19;56(7):957–970. doi: 10.1021/acs.biochem.6b00888

Figure 6.

Figure 6

HR-HRPF protection suggests stabilization of the helix α1–helix α5 interaction upon binding of b12 to helix α5. Helix α1 of the C1 domain (green) shows protection of four residues: M95 and W96 in the loop at the N-terminus of helix α1 and M99 and M104 within helix α1. The sole residue probed in helix α5, M475, interacts directly with a CDR loop of the b12 heavy chain (dark gray), with helix α5 (light gray) packing against the N-terminus of helix α1. Residues that showed >80% protection from HR-HRPF upon b12 binding are colored red. Residues that showed between 40 and 80% protection from HR-HRPF upon b12 binding are colored orange. Residues that showed statistically significant protection from HR-HRPF of <40% are colored yellow. Residues showing no protection from HR-HRPF upon b12 binding are colored blue.