Cargando…
Signature of Pareto optimization in the Escherichia coli proteome
Proteins have coevolved with cellular environments to improve or preserve their functions, maintaining at the same time the degree of hydrophobicity necessary to fold correctly and enough solubility to perform their biological roles. Here, we study the Escherichia coli proteome using a Pareto front...
Autores principales: | Koçillari, Loren, Fariselli, Piero, Trovato, Antonio, Seno, Flavio, Maritan, Amos |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Nature Publishing Group UK
2018
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6002381/ https://www.ncbi.nlm.nih.gov/pubmed/29904084 http://dx.doi.org/10.1038/s41598-018-27287-3 |
Ejemplares similares
-
Insight into the Structure of Amyloid Fibrils from the Analysis of Globular Proteins
por: Trovato, Antonio, et al.
Publicado: (2006) -
Homeostatic plasticity and emergence of functional networks in a whole-brain model at criticality
por: Rocha, Rodrigo P., et al.
Publicado: (2018) -
Pareto optimality between growth-rate and lag-time couples metabolic noise to phenotypic heterogeneity in Escherichia coli
por: Fuentes, Diego Antonio Fernandez, et al.
Publicado: (2021) -
Exploring the Universe of Protein Structures beyond the Protein Data Bank
por: Cossio, Pilar, et al.
Publicado: (2010) -
Criticality in Pareto Optimal Grammars?
por: Seoane, Luís F, et al.
Publicado: (2020)