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. Author manuscript; available in PMC: 2010 Sep 1.
Published in final edited form as: J Biomol NMR. 2009 Jul 31;45(1-2):85–98. doi: 10.1007/s10858-009-9340-0

Figure 7.

Figure 7

Structural dependence of conformational dynamics in HP67. Exchange broadened 13Cα and 13C methyl groups are mapped onto the structure of HP67. (a) Atoms are colored to correlate with the classifications depicted in Figs. 5 and 6; thus, green, blue and brown spheres represent residues that are fully disordered, retain native-like interactions and have non-native-like conformations in the intermediate, respectively. As can be seen, two regions of residual interactions are maintained the intermediate: (i) at the interface of the N- and C-terminal subdomains and (ii) in the vicinity of His41. (b) 13Cα and 13C methyl groups affected by the fast process with kex = (4.2 ± 0.5) × 104 s−1 are mapped to the structure and color coded to reflect the magnitude of exchange broadening. Atoms for which Rex > 2.5 s−1are colored red, atoms for which 1 s−1 < Rex < 2.5 s−1 are orange, and atoms for which Rex < 1 s−1are colored yellow.