Výsledky vyhledávání - "Leandro G. Garcia"

Non-native interactions, effective contact order, and protein folding: A mutational investigation with the energetically frustrated hydrophobic model

Autor: Leandro G. Garcia, Werner Treptow, Marco Aurélio A. Barbosa, Antônio F. Pereira de Araújo

Publikováno v: Proteins: Structure, Function, and Bioinformatics. 49:167-180

By Monte Carlo simulations, we explored the effect of single mutations on the thermodynamics and kinetics of the folding of a two-dimensional, energetically frustrated, hydrophobic protein model. Φ-Value analysis, corroborated by simulations beginni

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::7e869b22249bd152ab8819f99db8af37
https://doi.org/10.1002/prot.10166

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Folding pathway dependence on energetic frustration and interaction heterogeneity for a three-dimensional hydrophobic protein model

Autor: Leandro G. Garcia, Antônio F. Pereira de Araújo

Publikováno v: Proteins. 62(1)

Monte Carlo simulations of a hydrophobic protein model of 40 monomers in the cubic lattice are used to explore the effect of energetic frustration and interaction heterogeneity on its folding pathway. The folding pathway is described by the dependenc

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1d9c1654238a547a6455d7e21927d8a2
https://pubmed.ncbi.nlm.nih.gov/16292745

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Entropy reduction effect imposed by hydrogen bond formation on protein folding cooperativity: Evidence from a hydrophobic minimalist model

Autor: Marco Aurélio A. Barbosa, Leandro G. Garcia, Antônio F. Pereira de Araújo

Publikováno v: Physical Review E. 72

Conformational restrictions imposed by hydrogen bond formation during protein folding are investigated by Monte Carlo simulations of a non-native-centric, two-dimensional, hydrophobic model in which the formation of favorable contacts is coupled to a

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d9055a22badebbd60ee416b81d1baa93
https://doi.org/10.1103/physreve.72.051903

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Non-native interactions, effective contact order, and protein folding: a mutational investigation with the energetically frustrated hydrophobic model

Autor: Werner L, Treptow, Marco Aurélio A, Barbosa, Leandro G, Garcia, Antônio F, Pereira de Araújo

Publikováno v: Proteins. 49(2)

By Monte Carlo simulations, we explored the effect of single mutations on the thermodynamics and kinetics of the folding of a two-dimensional, energetically frustrated, hydrophobic protein model. Phi-Value analysis, corroborated by simulations beginn

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::87fe490250168f1921dc10b1319c2555
https://pubmed.ncbi.nlm.nih.gov/12210998

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Folding simulations of a three-dimensional protein model with a nonspecific hydrophobic energy function

Autor: Treptow Wl, Leandro G. Garcia, de Araújo Af

Publikováno v: Physical Review E. 64

We show that a nonspecific hydrophobic energy function can produce protein-like folding behavior of a three-dimensional protein model of 40 monomers in the cubic lattice when the native conformation is chosen judiciously. We confirm that monomer insi

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::aa626eb54aa36dd50881fed250b55fec
https://doi.org/10.1103/physreve.64.011912

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