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- W2138081309 abstract "An off-lattice all-atom (except nonpolar hydrogen) model of proteins based on Gō-type discontinuous interactions is developed and applied to study the folding thermodynamics of fragment B of Staphylococcal protein A. Unlike simpler Cα based off-lattice models, which fold into a molten globule-like state from the coil state, the new model transits directly to the native state. The transition is strongly first-order-like and the dynamics of the native state is in approximate agreement with experimental data. The results suggest that a large well-packed solid core is the origin of the folding cooperativity of proteins." @default.
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- W2138081309 date "2002-01-19" @default.
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- W2138081309 title "Thermodynamics of an All-Atom Off-Lattice Model of the Fragment B of <i>Staphylococcal</i> Protein A: Implication for the Origin of the Cooperativity of Protein Folding" @default.
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- W2138081309 doi "https://doi.org/10.1021/jp013824r" @default.
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