Wide transition-state ensemble as key component for enzyme catalysis
Transition-state (TS) theory has provided the theoretical framework to explain the enormous rate accelerations of chemical reactions by enzymes. Given that proteins display large ensembles of conformations, unique TSs would pose a huge entropic bottleneck for enzyme catalysis. To shed light on this...
Saved in:
| Main Authors: | Gabriel E Jara, Francesco Pontiggia, Renee Otten, Roman V Agafonov, Marcelo A Martí, Dorothee Kern |
|---|---|
| Format: | Article |
| Language: | English |
| Published: |
eLife Sciences Publications Ltd
2025-02-01
|
| Series: | eLife |
| Subjects: | |
| Online Access: | https://elifesciences.org/articles/93099 |
| Tags: |
Add Tag
No Tags, Be the first to tag this record!
|
Similar Items
-
Binding Zinc and Oxo-Vanadium Insulin-Mimetic Complexes to Phosphatase Enzymes: Structure, Electronics and Implications
by: Victor V. Volkov, et al.
Published: (2025-03-01) -
Multiscale Molecular Dynamics Simulations with the MiMiC Framework
by: Andrea Levy, et al.
Published: (2025-04-01) -
Molecular dynamics model of mechanophore sensors for biological force measurement
by: Sumit Mittal, et al.
Published: (2025-01-01) -
Modeling UV/Vis Absorption Spectra of Food Colorants in Solution: Anthocyanins and Curcumin as Case Studies
by: Sara Gómez, et al.
Published: (2024-09-01) -
Investigating hemolysis, elevated liver enzymes and low platelet count in preeclampsia: A case‐control study in Ghana
by: Martin Awe Akilla, et al.
Published: (2024-08-01)