The water factor in the protein-folding problem
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| Formato: | Artículo científico |
| Lenguaje: | en |
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Sociedade Brasileira de Física
2004
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| _version_ | 1876449286063915008 |
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| author | L. F.O. Rocha |
| author_facet | L. F.O. Rocha |
| contents | The water factor in the protein-folding problem L. F.O. Rocha M. E. Pinto Tarragó A. Caliri Física, Astronomía y Matemáticas Globular proteins are produced as a linear chain of aminoacids in water solution in the cell and, in the sameaqueous environment, fold into their respective unique and functional native structures. In spite of this, manytheoretical studies have tried to explain the folding process in vacuum, but in this paper we adopt an alternativepoint of view: the folding problem of heteropolymers is analyzed from the solvent perspective. The thermodynamicsof the folding process is discussed for a non homogeneous system composed by the chain and solventtogether; hydrophobic effects, modulated by the polar/nonpolar attributes of the residue sequence and by itscorresponding steric specificities, are proposed as basic ingredients for the mechanisms of the folding process.These ideas are incorporated in both lattice and off-lattice models and treated by Monte Carlo simulations.Configurational and thermodynamical results are compared with properties of real proteins. The results suggestthat the folding problem of small globular protein can be considered as a process in which the mechanism toreach the native structure and the requirements for the globule stability are uncoupled. 2004 artículo científico 0103-9733 https://www.redalyc.org/articulo.oa?id=46434112 en http://www.redalyc.org/revista.oa?id=464 Brazilian Journal of Physics application/pdf Sociedade Brasileira de Física Brazilian Journal of Physics (Brasil) Num.1 Vol.34 |
| format | Artículo científico |
| id | redalyc_46434112 |
| institution | Redalyc |
| language | en |
| publishDate | 2004 |
| publisher | Sociedade Brasileira de Física |
| spellingShingle | The water factor in the protein-folding problem L. F.O. Rocha Física, Astronomía y Matemáticas The water factor in the protein-folding problem L. F.O. Rocha M. E. Pinto Tarragó A. Caliri Física, Astronomía y Matemáticas Globular proteins are produced as a linear chain of aminoacids in water solution in the cell and, in the sameaqueous environment, fold into their respective unique and functional native structures. In spite of this, manytheoretical studies have tried to explain the folding process in vacuum, but in this paper we adopt an alternativepoint of view: the folding problem of heteropolymers is analyzed from the solvent perspective. The thermodynamicsof the folding process is discussed for a non homogeneous system composed by the chain and solventtogether; hydrophobic effects, modulated by the polar/nonpolar attributes of the residue sequence and by itscorresponding steric specificities, are proposed as basic ingredients for the mechanisms of the folding process.These ideas are incorporated in both lattice and off-lattice models and treated by Monte Carlo simulations.Configurational and thermodynamical results are compared with properties of real proteins. The results suggestthat the folding problem of small globular protein can be considered as a process in which the mechanism toreach the native structure and the requirements for the globule stability are uncoupled. 2004 artículo científico 0103-9733 https://www.redalyc.org/articulo.oa?id=46434112 en http://www.redalyc.org/revista.oa?id=464 Brazilian Journal of Physics application/pdf Sociedade Brasileira de Física Brazilian Journal of Physics (Brasil) Num.1 Vol.34 |
| title | The water factor in the protein-folding problem |
| topic | Física, Astronomía y Matemáticas |
| url | https://www.redalyc.org/articulo.oa?id=46434112 |