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. Author manuscript; available in PMC: 2015 Oct 23.
Published in final edited form as: Solid State Nucl Magn Reson. 2014 Oct 29;70:1–14. doi: 10.1016/j.ssnmr.2014.10.003

Fig. 3.

Fig. 3

A representative lowest energy structure of statherin bound to the 100 face of HAP, obtained with RosettaSurface and consistent with SSNMR constraints. The N-terminus is helical and associated with the surface, while the C-terminus folds back on itself and is thought to serve a role in lubrication of bacterial binding. Reproduced with permission from Ref. [44]. Copyright 2014 American Chemical Society.