Add to ORKGLarge-scale all-atom explicit solvent MD simulations have been carried out on rhodanese folding in a series of chaperonin mutants for 200 ns. Our analysis of the properties during simulation suggests that the GroE
The biological function of chaperone complexes is to assist the folding of non-native proteins. The ...
The biological function of chaperone complexes is to assist the folding of non-native proteins. The ...
Bacterial chaperonin, GroEL, together with its co-chaperonin, GroES, facilitates the folding of a va...
Incorrect folding of proteins in the macromolecular crowding environment in living cells would cause...
Chaperonins are known to facilitate the productive folding of numerous misfolded proteins. Despite t...
Chaperonins are known to facilitate the productive folding of numerous misfolded proteins. Despite t...
AbstractEncapsulation of proteins in chaperonins is an important mechanism by which the cell prevent...
AbstractCurrently, one of the most serious problems in protein-folding simulations for de novo struc...
The cylindrical chaperonin GroEL and its lid-shaped cofactor GroES of Escherichia coil have an essen...
The bacterial chaperonin GroEL/GroES assists folding of a broad spectrum of denatured and misfolded ...
Molecular chaperones are known to be essential for avoiding protein aggregation in vivo, but it is s...
Bacterial chaperonin, GroEL, together with its co-chaperonin, GroES, facilitates the folding of a va...
Bacterial chaperonin, GroEL, together with its co-chaperonin, GroES, facilitates the folding of a va...
AbstractThe bacterial chaperonin GroEL/GroES assists folding of a broad spectrum of denatured and mi...
Bacterial chaperonin, GroEL, together with its co-chaperonin, GroES, facilitates the folding of a va...
The biological function of chaperone complexes is to assist the folding of non-native proteins. The ...
The biological function of chaperone complexes is to assist the folding of non-native proteins. The ...
Bacterial chaperonin, GroEL, together with its co-chaperonin, GroES, facilitates the folding of a va...
Incorrect folding of proteins in the macromolecular crowding environment in living cells would cause...
Chaperonins are known to facilitate the productive folding of numerous misfolded proteins. Despite t...
Chaperonins are known to facilitate the productive folding of numerous misfolded proteins. Despite t...
AbstractEncapsulation of proteins in chaperonins is an important mechanism by which the cell prevent...
AbstractCurrently, one of the most serious problems in protein-folding simulations for de novo struc...
The cylindrical chaperonin GroEL and its lid-shaped cofactor GroES of Escherichia coil have an essen...
The bacterial chaperonin GroEL/GroES assists folding of a broad spectrum of denatured and misfolded ...
Molecular chaperones are known to be essential for avoiding protein aggregation in vivo, but it is s...
Bacterial chaperonin, GroEL, together with its co-chaperonin, GroES, facilitates the folding of a va...
Bacterial chaperonin, GroEL, together with its co-chaperonin, GroES, facilitates the folding of a va...
AbstractThe bacterial chaperonin GroEL/GroES assists folding of a broad spectrum of denatured and mi...
Bacterial chaperonin, GroEL, together with its co-chaperonin, GroES, facilitates the folding of a va...
The biological function of chaperone complexes is to assist the folding of non-native proteins. The ...
The biological function of chaperone complexes is to assist the folding of non-native proteins. The ...
Bacterial chaperonin, GroEL, together with its co-chaperonin, GroES, facilitates the folding of a va...