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. Author manuscript; available in PMC: 2010 Jul 16.
Published in final edited form as: Biochemistry. 2007 Dec 23;47(3):893–901. doi: 10.1021/bi701737f

Figure 2. Mobility of HNMT during MD.

Figure 2

(A) Cα-RMS fluctuations (Å) per residue from the 105T (green) and 105I (blue) MD simulations at 37°C. Cα-RMSFs were calculated relative to the average structure over the last 10 ns of each simulation. Experimental B-factors of the 105T HNMT crystal structure (2AOT, (28)) are colored in black. (B) Cα-RMSF difference plot for the HNMT simulations. Positive and negative values indicate greater overall fluctuations in the 105T and 105I HNMT proteins, respectively. Secondary structural elements are depicted as Inline graphic for α-helices, and Inline graphic for β-strands, and are colored to match the SAM- and histamine-binding domains shown in Figure 1. * = residue 105.