Computational Modeling of Allosteric Regulation in the Hsp90 Chaperones: A Statistical Ensemble Analysis of Protein Structure Networks and Allosteric Communications
Figure 5
The Force Constant Stability Analysis of the ADP-bound HtpG Chaperone.
(A) The residue-based force constant profile of the ADP-bound HtpG structure. The NTD residues are in green, MD residues are in blue, and CTD residues are in red. The residue-based dynamic profiles are annotated using the residue numbering in the original crystal structure [56]. The peaks of the force constant profiles corresponding to functionally important residues are indicated by arrows and annotated. Functional residues corresponding to the peaks in the force constant distribution are mapped onto the domain-colored crystal structure of ADP-HtpG (B) and onto the functional dynamics profile of ADP-HtpG (C). Functional residues are annotated and shown in spheres and colored as in Figure 4.