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• W2064867315 startingPage "415106" @default.
• W2064867315 abstract "The process of protein folding from an unfolded state to a biologically active, folded conformation is governed by many parameters e.g the sequence of amino acids, intermolecular interactions, the solvent, temperature and chaperon molecules. Our study, based on random matrix modeling of the interactions, shows however that the evolution of the statistical measures e.g Gibbs free energy, heat capacity, entropy is single parametric. The information can explain the selection of specific folding pathways from an infinite number of possible ways as well as other folding characteristics observed in computer simulation studies." @default.
• W2064867315 created "2016-06-24" @default.
• W2064867315 creator A5041244985 @default.
• W2064867315 date "2010-09-30" @default.
• W2064867315 modified "2023-09-25" @default.
• W2064867315 title "Thermodynamics of protein folding: a random matrix formulation" @default.
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• W2064867315 doi "https://doi.org/10.1088/0953-8984/22/41/415106" @default.
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