Cargando…
The relationship between chain connectivity and domain stability in the equilibrium and kinetic folding mechanisms of dihydrofolate reductase from E.coli
The role of domains in defining the equilibrium and kinetic folding properties of dihydrofolate reductase (DHFR) from Escherichia coli was probed by examining the thermodynamic and kinetic properties of a set of variants in which the chain connectivity in the discontinuous loop domain (DLD) and the...
Autores principales: | Svensson, Anna-Karin E., Zitzewitz, Jill A., Matthews, C.Robert, Smith, Virginia F. |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Oxford University Press
2006
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5441858/ https://www.ncbi.nlm.nih.gov/pubmed/16452118 http://dx.doi.org/10.1093/protein/gzj017 |
Ejemplares similares
-
Side Chain Conformational Averaging in Human Dihydrofolate
Reductase
por: Tuttle, Lisa M., et al.
Publicado: (2014) -
Tales of Dihydrofolate Binding to R67 Dihydrofolate
Reductase
por: Duff, Michael R., et al.
Publicado: (2015) -
FtsH degrades dihydrofolate reductase by recognizing a partially folded species
por: Morehouse, Juhee P., et al.
Publicado: (2022) -
Cryo‐kinetics Reveal Dynamic Effects on the Chemistry of Human Dihydrofolate Reductase
por: Adesina, Aduragbemi S., et al.
Publicado: (2021) -
Adaptations for Pressure and Temperature in Dihydrofolate Reductases
por: Penhallurick, Ryan W., et al.
Publicado: (2021)