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- W2055140399 endingPage "267" @default.
- W2055140399 startingPage "255" @default.
- W2055140399 abstract "A model of hydrophobic collapse, which is treated as the driving force for protein folding, is presented. This model is the superposition of three models commonly used in protein structure prediction: (1) 'oil-drop' model introduced by Kauzmann, (2) a lattice model introduced to decrease the number of degrees of freedom for structural changes and (3) a model of the formation of hydrophobic core as a key feature in driving the folding of proteins. These three models together helped to develop the idea of a fuzzy-oil-drop as a model for an external force field of hydrophobic character mimicking the hydrophobicity-differentiated environment for hydrophobic collapse. All amino acids in the polypeptide interact pair-wise during the folding process (energy minimization procedure) and interact with the external hydrophobic force field defined by a three-dimensional Gaussian function. The value of the Gaussian function usually interpreted as a probability distribution is treated as a normalized hydrophobicity distribution, with its maximum in the center of the ellipsoid and decreasing proportionally with the distance versus the center. The fuzzy-oil-drop is elastic and changes its shape and size during the simulated folding procedure." @default.
- W2055140399 created "2016-06-24" @default.
- W2055140399 creator A5027144155 @default.
- W2055140399 creator A5033579800 @default.
- W2055140399 creator A5087239926 @default.
- W2055140399 date "2006-08-01" @default.
- W2055140399 modified "2023-09-29" @default.
- W2055140399 title "Hydrophobic collapse in (in silico) protein folding" @default.
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- W2055140399 doi "https://doi.org/10.1016/j.compbiolchem.2006.04.007" @default.