Polypeptide foldings obtained with effective pair potentials.

P Pliego-Pastrana; M D Carbajal-Tinoco

doi:10.1063/1.1942492

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Polypeptide foldings obtained with effective pair potentials.

P Pliego-Pastrana·M D Carbajal-Tinoco

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Abstract

We present a model of protein folding which is based on a potential function that describes the effective interaction between two amino acids (alanines, in this case). Our model is consistent with the formation of two important secondary structures, namely, an alpha-helix and a beta-ladder. In each case, we estimate the density of states using a random walk in energy space. This function allows the direct calculation of certain thermodynamic properties. By means of the configurational temperature, we also verify that the obtained polypeptides are in their native state.

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Alanine Algorithms Hydrogen Bonding Neutrons Peptides Protein Conformation Protein Folding Scattering, Radiation Thermodynamics Journal Article Research Support, Non-U.S. Gov't

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P Pliego-Pastrana, M D Carbajal-Tinoco. 2005-06-22. Polypeptide foldings obtained with effective pair potentials.. https://doi.org/10.1063/1.1942492

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