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. Author manuscript; available in PMC: 2013 Aug 1.
Published in final edited form as: Nat Chem Biol. 2012 Dec 9;9(2):81–83. doi: 10.1038/nchembio.1138

Figure 2. Conformational dynamics of the ligase enzyme 10C.

Figure 2

(a) Mapping of the heteronuclear NOEs (proxy for fast dynamics on a picosecond-nanosecond time scale) on ligase 10C. Residues involved in zinc coordination are labeled. (b) Mapping of the exchange rates (Rex) obtained from relaxation dispersion measurements as a proxy for slow dynamics (microsecond-millisecond time scale). The color gradient and thickness of the backbone indicate that the ligase fast dynamics is located mostly in the unstructured loop, while the slow dynamics is located mostly in the region N-terminal to the Zn-II site (residues 46–53) and is potentially correlated to catalytic activity.