Cargando…
Deciphering the Dynamics of Non-Covalent Interactions Affecting Thermal Stability of a Protein: Molecular Dynamics Study on Point Mutant of Thermus thermophilus Isopropylmalate Dehydrogenase
Thermus thermophilius isopropylmalate dehydrogenase catalyzes oxidative decarboxylation and dehydrogenation of isopropylmalate. Substitution of leucine to alanine at position 172 enhances the thermal stability among the known point mutants. Exploring the dynamic properties of non-covalent interactio...
Autores principales: | Sharma, Reetu, Sastry, G. Narahari |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Public Library of Science
2015
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4689552/ https://www.ncbi.nlm.nih.gov/pubmed/26657745 http://dx.doi.org/10.1371/journal.pone.0144294 |
Ejemplares similares
-
Crystal structure of Thermus thermophilus methylenetetrahydrofolate dehydrogenase and determinants of thermostability
por: Maiello, Fernando, et al.
Publicado: (2020) -
Tiamulin-Resistant Mutants of the Thermophilic Bacterium Thermus thermophilus
por: Killeavy, Erin E., et al.
Publicado: (2020) -
The quaternary structure of Thermus thermophilus aldehyde dehydrogenase is stabilized by an evolutionary distinct C-terminal arm extension
por: Hayes, Kevin, et al.
Publicado: (2018) -
Functional Impact of the N-terminal Arm of Proline Dehydrogenase from Thermus thermophilus
por: Huijbers, Mieke M. E., et al.
Publicado: (2018) -
Proline dehydrogenase from Thermus thermophilus does not discriminate between FAD and FMN as cofactor
por: Huijbers, Mieke M. E., et al.
Publicado: (2017)