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. 2019 Sep 27;9(10):543. doi: 10.3390/biom9100543

Figure 3.

Figure 3

Comparative surface features of linker motifs of PfHsp70-1 (canonical Hsp70) and PfHsp70-z (Hsp110). PfHsp70-z, an Hsp110, possesses a more hydrophilic linker surface interface (A) as opposed to the more hydrophobic linker surface of canonical Hsp70, represented by PfHsp70-1 (B). The glutamate residues on the surface of PfHsp70-z account for a negatively charged linker surface (C) as opposed to that of PfHsp70-1 which is mostly neutral (D). The linker of PfHsp70-z (Hsp110) (E) possesses more hydrogen binding sites as compared to the linker for the canonical Hsp70 (PfHsp70-1) (F).