Contact map of α-lactalbumin at pH 1, 3, 7, 9, and 11. The contact map of the proteins in crystal structure is also provided for comparison.
Residue average mean square fluctuations (MSFs) of C α atoms (shown in lines) and normalized solvent accessibility (shown in bars) of α-lactalbumin at different pHs. MSFs of tryptophan residues are highlighted as red circles.
Time evolution of secondary structures in α-lactalbumin during simulations at different pH. DSSP annotations used are provided at the top of the graph. H refers to α-helix, G refers to 310-helix, I refers to π-helix, B refers to residue in isolated β-strand, E refers to residue in β-strand participate in β-sheet, T refers to hydrogen bonded turn, S refers to bend, and C refers to random coil.
Structural parameters describing the structure of α-lactalbumin at different pH simulations: (i) Root-Mean-Square Deviation (RMSD) from the crystallographic structure of C α carbon atoms and all atoms, (ii) Radius of Gyration (R G ) of α-lactalbumin, (iii) Total Solvent Accessible Surface Area (SASA), (iv) Number of Native Contacts (NC), and (v) Number of Total Contacts (TC) a .
Fractal dimension (D 1 and D 2) of α-lactalbumin at different pH values.
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