Roles of hydrophobic and hydrophilic forces on maintaining amyloid-prone cystatin structural stability

Figures & data

Figure 1 The cC monomeric structure with selected residues Ile66, Ile108 in the hydrophobic core, and Val55 in Loop 1.

Figure 2 Time dependence of the RMSD from the total amino acid of cC for the Cα (A) and the hydrophobic core of cC for the backbone (B) in the 10 ns MD simulation.

Table 1. The intramolecular HBs number in mutants and wild-type cC.

Mutants	Whole protein	Hydrophobic core	β2 and β3	Residue 55
WT	64.59580	19.36945	12.70	.18
I66Q	64.08124	17.88726	11.52	.15
V55 N/I66Q	69.63092	18.12761	13.64	.53
V55D/I66Q	71.25947	19.92988	13.89	.35
Note: The data are the average values in the last 7 ns of the simulations.