Cargando…
High-throughput thermal denaturation of tryptophanyl-tRNA synthetase combinatorial mutants reveals high-order energetic coupling determinants of conformational stability
Landscape descriptions provide a framework for identifying functionally significant dynamic linkages in proteins but cannot supply details. Rate measurements of combinatorial mutations can implicate dynamic linkages in catalysis. A major difficulty is filtering dynamic linkages from the vastly more...
Autores principales: | Weinreb, Violetta, Weinreb, Gabriel, Carter, Charles W. |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
American Crystallographic Association
2023
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10449480/ https://www.ncbi.nlm.nih.gov/pubmed/37637481 http://dx.doi.org/10.1063/4.0000182 |
Ejemplares similares
-
Microcalorimetry reveals multi-state thermal denaturation of G. stearothermophilus tryptophanyl-tRNA synthetase
por: Chandrasekaran, Srinivas Niranj, et al.
Publicado: (2023) -
Histidyl-tRNA Synthetase Urzymes: CLASS I AND II AMINOACYL tRNA SYNTHETASE URZYMES HAVE COMPARABLE CATALYTIC ACTIVITIES FOR COGNATE AMINO ACID ACTIVATION
por: Li, Li, et al.
Publicado: (2011) -
Crystal structure of Pyrococcus horikoshii tryptophanyl-tRNA synthetase and structure-based phylogenetic analysis suggest an archaeal origin of tryptophanyl-tRNA synthetase
por: Dong, Xianchi, et al.
Publicado: (2010) -
Tryptophanyl-tRNA Synthetase as a Potential Therapeutic Target
por: Ahn, Young Ha, et al.
Publicado: (2021) -
Tryptophan-Starved Human Cells Overexpressing Tryptophanyl-tRNA Synthetase Enhance High-Affinity Tryptophan Uptake via Enzymatic Production of Tryptophanyl-AMP
por: Yokosawa, Takumi, et al.
Publicado: (2023)