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Figure 8
Amide H/D exchange indicates that T-state HuDeoxyHb has greater flexibility, while R-state EqCNmetHb displays less exchange in the αβ dimer interface. Superimposed on the ribbon figures of T-state HuDeoxyHb (a) and R-state EqCNmetHb (b) are the positions of non-exchanged backbone amide H atoms (magenta) indicating regions of minimal flexibility. The T state has regions of non-exchange in the α1β2 tetramer interface, while the R state has a more extensive region of non-exchange in the α1β1 dimer interface. (c) shows the H/D exchange related to the primary sequence, with T1 and T2 indicating the two dimers of the T-state HuDeoxyHb model and R indicating the R-state EqCNmetHb model, and is color-coded as follows: non-exchanged in magenta (occupancy range −0.56 to 0.0), partially exchanged in cyan (occupancy range 0.0–0.6) and fully exchanged in green (occupancy range 0.6–1.0); prolines indicated in red lack backbone amide protons. The secondary structure and interface contacts are aligned with the sequence.

Journal logoSTRUCTURAL
BIOLOGY
ISSN: 2059-7983
Volume 72| Part 7| July 2016| Pages 892-903
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