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Capturing molten globule state of α-lactalbumin through constant pH molecular dynamics simulations
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Image of FIG. 1.
FIG. 1.

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.

Image of FIG. 2.
FIG. 2.

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.

Image of FIG. 3.
FIG. 3.

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.


Generic image for table
Table I.

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 .

Generic image for table
Table II.

Fractal dimension (D 1 and D 2) of α-lactalbumin at different pH values.


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752b84549af89a08dbdd7fdb8b9568b5 journal.articlezxybnytfddd
Scitation: Capturing molten globule state of α-lactalbumin through constant pH molecular dynamics simulations