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. 2011 May 11;108(22):9078–9083. doi: 10.1073/pnas.1105682108

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Fig. 1. — Sensitivity of N-state ¹⁵N chemical shifts and R_ex relaxation rates to changes in pH. (A) Magnitude of ¹⁵N chemical shift changes between pH 5.9 and 4.95, color-coded to highlight His (red); residues contacting His (orange); and residues contacting the disordered F helix, FG loop, and N-terminal region of helix G (blue); other residues are colored green. The solid black rectangles at the top of the figure depict helices in apoMb based on a TALOS+ (30) analysis of , ¹⁵N, ¹³CO, , and chemical shifts (6), whereas the boundaries of the F, G, and H helices in holoMb are shown as open rectangles. (B) ¹⁵N R_ex (at a static magnetic field of 11.7 T) of deuterated apoMb at 35 °C; pH 5.9 (blue), pH 4.9 (red). R_ex was estimated from the difference in R_2eff at the lowest and highest 1/τ_cp values. The green squares on the horizontal axis indicate contact sites with helix F in holoMb, and the circles identify His residues. Yellow squares indicate the N-terminal region of helix G.

Inline graphic — Sensitivity of N-state ¹⁵N chemical shifts and R_ex relaxation rates to changes in pH. (A) Magnitude of ¹⁵N chemical shift changes between pH 5.9 and 4.95, color-coded to highlight His (red); residues contacting His (orange); and residues contacting the disordered F helix, FG loop, and N-terminal region of helix G (blue); other residues are colored green. The solid black rectangles at the top of the figure depict helices in apoMb based on a TALOS+ (30) analysis of , ¹⁵N, ¹³CO, , and chemical shifts (6), whereas the boundaries of the F, G, and H helices in holoMb are shown as open rectangles. (B) ¹⁵N R_ex (at a static magnetic field of 11.7 T) of deuterated apoMb at 35 °C; pH 5.9 (blue), pH 4.9 (red). R_ex was estimated from the difference in R_2eff at the lowest and highest 1/τ_cp values. The green squares on the horizontal axis indicate contact sites with helix F in holoMb, and the circles identify His residues. Yellow squares indicate the N-terminal region of helix G.