Cargando…
Substrate Binding Stiffens Aspartate Aminotransferase by Altering the Enzyme Picosecond Vibrational Dynamics
[Image: see text] Protein dynamics on various time scales from femtoseconds to milliseconds impacts biological function by driving proteins to conformations conducive to ligand binding and creating functional states in enzyme catalysis. Neutron vibrational spectroscopy carried out by measuring inela...
Autores principales: | Dajnowicz, Steven, Cheng, Yongqiang, Daemen, Luke L., Weiss, Kevin L., Gerlits, Oksana, Mueser, Timothy C., Kovalevsky, Andrey |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
American Chemical Society
2020
|
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7408236/ https://www.ncbi.nlm.nih.gov/pubmed/32775880 http://dx.doi.org/10.1021/acsomega.0c01900 |
Ejemplares similares
-
An N⋯H⋯N low-barrier hydrogen bond preorganizes the catalytic site of aspartate aminotransferase to facilitate the second half-reaction
por: Drago, Victoria N., et al.
Publicado: (2022) -
Direct visualization of critical hydrogen atoms in a pyridoxal 5′-phosphate enzyme
por: Dajnowicz, Steven, et al.
Publicado: (2017) -
Insights into the Phosphoryl Transfer Catalyzed by
cAMP-Dependent Protein Kinase: An X-ray Crystallographic Study
of Complexes with Various Metals and Peptide Substrate SP20
por: Gerlits, Oksana, et al.
Publicado: (2013) -
Room temperature crystallography of human acetylcholinesterase bound to a substrate analogue 4K-TMA: Towards a neutron structure
por: Gerlits, Oksana, et al.
Publicado: (2021) -
Revealing protonation states and tracking substrate in serine hydroxymethyltransferase with room-temperature X-ray and neutron crystallography
por: Drago, Victoria N., et al.
Publicado: (2023)