Cargando…
Positive and Negative Design in Stability and Thermal Adaptation of Natural Proteins
The aim of this work is to elucidate how physical principles of protein design are reflected in natural sequences that evolved in response to the thermal conditions of the environment. Using an exactly solvable lattice model, we design sequences with selected thermal properties. Compositional analys...
Autores principales: | Berezovsky, Igor N, Zeldovich, Konstantin B, Shakhnovich, Eugene I |
---|---|
Formato: | Texto |
Lenguaje: | English |
Publicado: |
Public Library of Science
2007
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1829478/ https://www.ncbi.nlm.nih.gov/pubmed/17381236 http://dx.doi.org/10.1371/journal.pcbi.0030052 |
Ejemplares similares
-
Protein and DNA Sequence Determinants of Thermophilic Adaptation
por: Zeldovich, Konstantin B, et al.
Publicado: (2007) -
Entropic Stabilization of Proteins and Its Proteomic Consequences
por: Berezovsky, Igor N, et al.
Publicado: (2005) -
A First-Principles Model of Early Evolution: Emergence of Gene Families, Species, and Preferred Protein Folds
por: Zeldovich, Konstantin B, et al.
Publicado: (2007) -
Positively Selected Sites in Cetacean Myoglobins Contribute to Protein Stability
por: Dasmeh, Pouria, et al.
Publicado: (2013) -
Thermal Stabilization of Dihydrofolate Reductase Using Monte Carlo Unfolding Simulations and Its Functional Consequences
por: Tian, Jian, et al.
Publicado: (2015)