Cargando…
The free energy for hydrolysis of a microtubule-bound nucleotide triphosphate is near zero: all of the free energy for hydrolysis is stored in the microtubule lattice [published erratum appears in J Cell Biol 1995 Apr;129(2):549]
The standard free energy for hydrolysis of the GTP analogue guanylyl- (a,b)-methylene-diphosphonate (GMPCPP), which is -5.18 kcal in solution, was found to be -3.79 kcal in tubulin dimers, and only -0.90 kcal in tubulin subunits in microtubules. The near-zero change in standard free energy for GMPCP...
Formato: | Texto |
---|---|
Lenguaje: | English |
Publicado: |
The Rockefeller University Press
1994
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2120239/ https://www.ncbi.nlm.nih.gov/pubmed/7962059 |
Ejemplares similares
-
Unveiling the catalytic mechanism of GTP hydrolysis in microtubules
por: Beckett, Daniel, et al.
Publicado: (2023) -
Kinesin is the motor for microtubule-mediated Golgi-to-ER membrane traffic [published errata appear in J Cell Biol 1995 Mar;128(5):following 988 and 1995 May;129(3):893]
Publicado: (1995) -
The hydrolysis of proteins by microwave energy
por: Margolis, Sam A., et al.
Publicado: (1991) -
The speed of GTP hydrolysis determines GTP cap size and controls microtubule stability
por: Roostalu, Johanna, et al.
Publicado: (2020) -
Mechanism of Guanosine Triphosphate Hydrolysis by the Visual Proteins Arl3-RP2: Free Energy Reaction Profiles Computed with Ab Initio Type QM/MM Potentials
por: Khrenova, Maria G., et al.
Publicado: (2021)