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Solvent–amino acid interaction energies in three‐dimensional‐lattice Monte Carlo simulations of a model 27‐mer protein: Folding thermodynamics and kinetics
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| Zeitschriftentitel: | Protein Science |
|---|---|
| Personen und Körperschaften: | , , |
| In: | Protein Science, 13, 2004, 2, S. 358-369 |
| Format: | E-Article |
| Sprache: | Englisch |
| veröffentlicht: |
Wiley
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| Schlagwörter: |
| author_facet |
Leonhard, Kai Prausnitz, John M. Radke, Clayton J. Leonhard, Kai Prausnitz, John M. Radke, Clayton J. |
|---|---|
| author |
Leonhard, Kai Prausnitz, John M. Radke, Clayton J. |
| spellingShingle |
Leonhard, Kai Prausnitz, John M. Radke, Clayton J. Protein Science Solvent–amino acid interaction energies in three‐dimensional‐lattice Monte Carlo simulations of a model 27‐mer protein: Folding thermodynamics and kinetics Molecular Biology Biochemistry |
| author_sort |
leonhard, kai |
| spelling |
Leonhard, Kai Prausnitz, John M. Radke, Clayton J. 0961-8368 1469-896X Wiley Molecular Biology Biochemistry http://dx.doi.org/10.1110/ps.03198204 <jats:title>Abstract</jats:title><jats:p>Amino acid residue–solvent interactions are required for lattice Monte Carlo simulations of model proteins in water. In this study, we propose an interaction‐energy scale that is based on the interaction scale by Miyazawa and Jernigan. It permits systematic variation of the amino acid–solvent interactions by introducing a contrast parameter for the hydrophobicity, <jats:italic>C</jats:italic><jats:sub><jats:italic>s</jats:italic></jats:sub>, and a mean attraction parameter for the amino acids, ω. Changes in the interaction energies strongly affect many protein properties. We present an optimized energy parameter set for best representing realistic behavior typical for many proteins (fast folding and high cooperativity for single chains). Our optimal parameters feature a much weaker hydrophobicity contrast and mean attraction than does the original interaction scale. The proposed interaction scale is designed for calculating the behavior of proteins in bulk and at interfaces as a function of solvent characteristics, as well as protein size and sequence.</jats:p> Solvent–amino acid interaction energies in three‐dimensional‐lattice Monte Carlo simulations of a model 27‐mer protein: Folding thermodynamics and kinetics Protein Science |
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Protein Science |
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| title |
Solvent–amino acid interaction energies in three‐dimensional‐lattice Monte Carlo simulations of a model 27‐mer protein: Folding thermodynamics and kinetics |
| title_unstemmed |
Solvent–amino acid interaction energies in three‐dimensional‐lattice Monte Carlo simulations of a model 27‐mer protein: Folding thermodynamics and kinetics |
| title_full |
Solvent–amino acid interaction energies in three‐dimensional‐lattice Monte Carlo simulations of a model 27‐mer protein: Folding thermodynamics and kinetics |
| title_fullStr |
Solvent–amino acid interaction energies in three‐dimensional‐lattice Monte Carlo simulations of a model 27‐mer protein: Folding thermodynamics and kinetics |
| title_full_unstemmed |
Solvent–amino acid interaction energies in three‐dimensional‐lattice Monte Carlo simulations of a model 27‐mer protein: Folding thermodynamics and kinetics |
| title_short |
Solvent–amino acid interaction energies in three‐dimensional‐lattice Monte Carlo simulations of a model 27‐mer protein: Folding thermodynamics and kinetics |
| title_sort |
solvent–amino acid interaction energies in three‐dimensional‐lattice monte carlo simulations of a model 27‐mer protein: folding thermodynamics and kinetics |
| topic |
Molecular Biology Biochemistry |
| url |
http://dx.doi.org/10.1110/ps.03198204 |
| publishDate |
2004 |
| physical |
358-369 |
| description |
<jats:title>Abstract</jats:title><jats:p>Amino acid residue–solvent interactions are required for lattice Monte Carlo simulations of model proteins in water. In this study, we propose an interaction‐energy scale that is based on the interaction scale by Miyazawa and Jernigan. It permits systematic variation of the amino acid–solvent interactions by introducing a contrast parameter for the hydrophobicity, <jats:italic>C</jats:italic><jats:sub><jats:italic>s</jats:italic></jats:sub>, and a mean attraction parameter for the amino acids, ω. Changes in the interaction energies strongly affect many protein properties. We present an optimized energy parameter set for best representing realistic behavior typical for many proteins (fast folding and high cooperativity for single chains). Our optimal parameters feature a much weaker hydrophobicity contrast and mean attraction than does the original interaction scale. The proposed interaction scale is designed for calculating the behavior of proteins in bulk and at interfaces as a function of solvent characteristics, as well as protein size and sequence.</jats:p> |
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| author | Leonhard, Kai, Prausnitz, John M., Radke, Clayton J. |
| author_facet | Leonhard, Kai, Prausnitz, John M., Radke, Clayton J., Leonhard, Kai, Prausnitz, John M., Radke, Clayton J. |
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| description | <jats:title>Abstract</jats:title><jats:p>Amino acid residue–solvent interactions are required for lattice Monte Carlo simulations of model proteins in water. In this study, we propose an interaction‐energy scale that is based on the interaction scale by Miyazawa and Jernigan. It permits systematic variation of the amino acid–solvent interactions by introducing a contrast parameter for the hydrophobicity, <jats:italic>C</jats:italic><jats:sub><jats:italic>s</jats:italic></jats:sub>, and a mean attraction parameter for the amino acids, ω. Changes in the interaction energies strongly affect many protein properties. We present an optimized energy parameter set for best representing realistic behavior typical for many proteins (fast folding and high cooperativity for single chains). Our optimal parameters feature a much weaker hydrophobicity contrast and mean attraction than does the original interaction scale. The proposed interaction scale is designed for calculating the behavior of proteins in bulk and at interfaces as a function of solvent characteristics, as well as protein size and sequence.</jats:p> |
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| imprint | Wiley, 2004 |
| imprint_str_mv | Wiley, 2004 |
| institution | DE-D275, DE-Bn3, DE-Brt1, DE-Zwi2, DE-D161, DE-Gla1, DE-Zi4, DE-15, DE-Pl11, DE-Rs1, DE-105, DE-14, DE-Ch1, DE-L229 |
| issn | 0961-8368, 1469-896X |
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| language | English |
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| mega_collection | Wiley (CrossRef) |
| physical | 358-369 |
| publishDate | 2004 |
| publishDateSort | 2004 |
| publisher | Wiley |
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| recordtype | ai |
| series | Protein Science |
| source_id | 49 |
| spelling | Leonhard, Kai Prausnitz, John M. Radke, Clayton J. 0961-8368 1469-896X Wiley Molecular Biology Biochemistry http://dx.doi.org/10.1110/ps.03198204 <jats:title>Abstract</jats:title><jats:p>Amino acid residue–solvent interactions are required for lattice Monte Carlo simulations of model proteins in water. In this study, we propose an interaction‐energy scale that is based on the interaction scale by Miyazawa and Jernigan. It permits systematic variation of the amino acid–solvent interactions by introducing a contrast parameter for the hydrophobicity, <jats:italic>C</jats:italic><jats:sub><jats:italic>s</jats:italic></jats:sub>, and a mean attraction parameter for the amino acids, ω. Changes in the interaction energies strongly affect many protein properties. We present an optimized energy parameter set for best representing realistic behavior typical for many proteins (fast folding and high cooperativity for single chains). Our optimal parameters feature a much weaker hydrophobicity contrast and mean attraction than does the original interaction scale. The proposed interaction scale is designed for calculating the behavior of proteins in bulk and at interfaces as a function of solvent characteristics, as well as protein size and sequence.</jats:p> Solvent–amino acid interaction energies in three‐dimensional‐lattice Monte Carlo simulations of a model 27‐mer protein: Folding thermodynamics and kinetics Protein Science |
| spellingShingle | Leonhard, Kai, Prausnitz, John M., Radke, Clayton J., Protein Science, Solvent–amino acid interaction energies in three‐dimensional‐lattice Monte Carlo simulations of a model 27‐mer protein: Folding thermodynamics and kinetics, Molecular Biology, Biochemistry |
| title | Solvent–amino acid interaction energies in three‐dimensional‐lattice Monte Carlo simulations of a model 27‐mer protein: Folding thermodynamics and kinetics |
| title_full | Solvent–amino acid interaction energies in three‐dimensional‐lattice Monte Carlo simulations of a model 27‐mer protein: Folding thermodynamics and kinetics |
| title_fullStr | Solvent–amino acid interaction energies in three‐dimensional‐lattice Monte Carlo simulations of a model 27‐mer protein: Folding thermodynamics and kinetics |
| title_full_unstemmed | Solvent–amino acid interaction energies in three‐dimensional‐lattice Monte Carlo simulations of a model 27‐mer protein: Folding thermodynamics and kinetics |
| title_short | Solvent–amino acid interaction energies in three‐dimensional‐lattice Monte Carlo simulations of a model 27‐mer protein: Folding thermodynamics and kinetics |
| title_sort | solvent–amino acid interaction energies in three‐dimensional‐lattice monte carlo simulations of a model 27‐mer protein: folding thermodynamics and kinetics |
| title_unstemmed | Solvent–amino acid interaction energies in three‐dimensional‐lattice Monte Carlo simulations of a model 27‐mer protein: Folding thermodynamics and kinetics |
| topic | Molecular Biology, Biochemistry |
| url | http://dx.doi.org/10.1110/ps.03198204 |