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. Author manuscript; available in PMC: 2019 Feb 28.
Published in final edited form as: Chem Rev. 2018 Jan 10;118(4):1691–1741. doi: 10.1021/acs.chemrev.7b00305

Figure 17.

Figure 17

Sample results from the TransComp web server. (a) Comparison between predicted and experimental ka values for 49 protein complexes. Ionic strengths were chosen to be close to a physiological value (i.e., 0.15 M) when possible. Reprinted with permission from ref 457. Copyright 2011 Elsevier. (b) Collage of structures for a subset of the 49 protein complexes. Protein structures were modified in two cases before TransComp calculations: for 40 (hirudin and thrombin), only the docking segment (shown in green ribbon) of hirudin was used; for 46 (ribonuclease A and inhibitor protein), the cleft of the inhibitor protein (red surface) was widened by a normal-mode analysis based on an elastic network model.