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. Author manuscript; available in PMC: 2010 Dec 31.
Published in final edited form as: J Phys Chem B. 2009 Dec 31;113(52):16669–16680. doi: 10.1021/jp9077213

Figure 5. Comparison of the slowest mode of ubiquitin at microsecond time-scale based on QHA0.5μs (computational) and EROS ensemble (experimental).

Figure 5

The modes are depicted in a movie like fashion, with subsequent conformations shown in lighter colors. Four regions of the protein are highlighted with different colors and labeled; these regions indicate large displacements. These motions involve a pincer-like motion involving β1-β2, C-terminal part of α1 helix and α1-β3 loops. The amplitudes of the motions are arbitrarily scaled for visualization, however, see text for comparison of the coverage of conformational landscape.