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Molecular simulation of surfactant-assisted protein refolding
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10.1063/1.1866052
/content/aip/journal/jcp/122/13/10.1063/1.1866052
http://aip.metastore.ingenta.com/content/aip/journal/jcp/122/13/10.1063/1.1866052
View: Figures

Figures

Image of FIG. 1.
FIG. 1.

Models of protein and surfactant. (a) The native state of the 20-bead protein: the H-beads form a compact hydrophobic core that is surrounded by the P beads. There are eight intramolecular hydrophobic interaction contacts in the native conformation. Labels in the P beads represent the sequence of the model protein chain. (b) One of the fully unfolded states of the 20-bead protein: there is no intramolecular hydrophobic interaction contact in the fully unfolded state of model protein. (c) Surfactant molecule.

Image of FIG. 2.
FIG. 2.

The changes of the average energy of the model protein as a function of the absolute reduced intramolecular hydrophobic interaction strength . represents the native state of model protein; represents the unfolded state of model protein; and represents 50% of the protein is in the denatured form.

Image of FIG. 3.
FIG. 3.

The energy and corresponding appearance frequency of conformations captured during the full run of simulation process as a function of the absolute intramolecular hydrophobic interaction strength in the absence of the surfactant. (a) ; (b) ; (c) ; (d) ; (e) ; (f) ; (g) ; (h) .

Image of FIG. 4.
FIG. 4.

Some conformations of identical energy of −6.

Image of FIG. 5.
FIG. 5.

The energy and corresponding appearance frequency of conformations captured during the full run of simulation process as a function of the absolute intramolecular hydrophobic interaction strength in the presence of the surfactant. (a) ; (b) ; (c) ; (d) ; (e) ; (f) ; (g) ; (h) .

Image of FIG. 6.
FIG. 6.

The mechanism of surfactant on facilitating the conformational transition in protein refolding. (a) Conformational transition probability without surfactant; (b) conformational transition probability with one surfactant molecule; (c) conformational transition probability with two surfactant molecules.

Image of FIG. 7.
FIG. 7.

Protein refolding yield with surfactants of different hydrophobicity at various values of the intramolecular hydrophobic interaction strength of protein.

Image of FIG. 8.
FIG. 8.

Protein refolding yield with different surfactant concentrations at various values of the hydrophobicity of surfactants .

Image of FIG. 9.
FIG. 9.

The “energy landscape” perspective of protein during folding process. (a) Isolate protein refolding at different intramolecular hydrophobic interaction strength ; (b) protein refolding at high value of with and without surfactant; (c) surfactant with different hydrophobicity assisted protein refolding; (d) a perspective of energy landscape of the model protein in the absence of surfactant and in the presence of surfactant.

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/content/aip/journal/jcp/122/13/10.1063/1.1866052
2005-04-01
2014-04-17
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752b84549af89a08dbdd7fdb8b9568b5 journal.articlezxybnytfddd
Scitation: Molecular simulation of surfactant-assisted protein refolding
http://aip.metastore.ingenta.com/content/aip/journal/jcp/122/13/10.1063/1.1866052
10.1063/1.1866052
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