Cargando…
Pressure Adaptations in Deep-Sea Moritella Dihydrofolate Reductases: Compressibility versus Stability
SIMPLE SUMMARY: Deep-sea organisms must have proteins that function under high hydrostatic pressure to survive. Adaptations used in proteins from “pressure-loving” piezophiles may include greater compressibility or greater stability against pressure-induced destabilization. However, while greater co...
Autores principales: | Penhallurick, Ryan W., Ichiye, Toshiko |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
MDPI
2021
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8614765/ https://www.ncbi.nlm.nih.gov/pubmed/34827204 http://dx.doi.org/10.3390/biology10111211 |
Ejemplares similares
-
Adaptations for Pressure and Temperature in Dihydrofolate Reductases
por: Penhallurick, Ryan W., et al.
Publicado: (2021) -
Effects of Pressure and Temperature on the Atomic Fluctuations of Dihydrofolate Reductase from a Psychropiezophile and a Mesophile
por: Huang, Qi, et al.
Publicado: (2019) -
Tales of Dihydrofolate Binding to R67 Dihydrofolate
Reductase
por: Duff, Michael R., et al.
Publicado: (2015) -
Complete Genome Sequence of the Deep-Sea Bacterium Moritella marina MP-1 (ATCC 15381)
por: Magin, Simon, et al.
Publicado: (2020) -
Thermal Adaptation of Dihydrofolate Reductase from
the Moderate Thermophile Geobacillus stearothermophilus
por: Guo, Jiannan, et al.
Publicado: (2014)