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.
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.
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) .
Some conformations of identical energy of −6.
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) .
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.
Protein refolding yield with surfactants of different hydrophobicity at various values of the intramolecular hydrophobic interaction strength of protein.
Protein refolding yield with different surfactant concentrations at various values of the hydrophobicity of surfactants .
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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