The results of minimal model calculations indicate that the stability and the kinetic accessibility of the native state of small globular proteins are controlled by few hot sites. By means of molecular dynamics simulations around the native conformation, which describe the protein and the surrounding solvent at the all-atom level, an accurate and compact energetic map of the native state of the protein is generated. This map is further simplified by means of an eigenvalue decomposition. The components of the eigenvector associated with the lowest eigenvalue indicate which hot sites are likely to be responsible for the stability and for the rapid folding of the protein. The comparison of the results of the model with the findings of mutagene...
The free-energy landscape of a small protein, the FBP 28 WW domain, has been explored using molecula...
Most proteins must fold to a well-defined structure with a minimal stability to perform their funct...
We present a theoretical framework for the study of the protein folding problem and apply it to the ...
The results of minimal model calculations indicate that the stability and the kinetic accessibility...
A new energy decomposition approach, aimed at identifying residues playing a folding key role, has b...
The native state can be considered as a unique conformation of the protein molecule with the lowest ...
The free-energy landscape of a small protein, the FBP 28 WW domain, has been explored using molecula...
The native state can be considered as a unique conformation of the protein molecule with the lowest ...
The free-energy landscape of a small protein, the FBP 28 WW domain, has been explored using molecula...
Herein, we present a novel Hamiltonian replica exchange protocol for classical molecular dynamics si...
The native state can be considered as a unique conformation of the protein molecule with the lowest ...
The free-energy landscape of a small protein, the FBP 28 WW domain, has been explored using molecula...
Herein, we present a novel Hamiltonian replica exchange protocol for classical molecular dynamics si...
The free-energy landscape of a small protein, the FBP 28 WW domain, has been explored using molecula...
The free-energy landscape of a small protein, the FBP 28 WW domain, has been explored using molecula...
The free-energy landscape of a small protein, the FBP 28 WW domain, has been explored using molecula...
Most proteins must fold to a well-defined structure with a minimal stability to perform their funct...
We present a theoretical framework for the study of the protein folding problem and apply it to the ...
The results of minimal model calculations indicate that the stability and the kinetic accessibility...
A new energy decomposition approach, aimed at identifying residues playing a folding key role, has b...
The native state can be considered as a unique conformation of the protein molecule with the lowest ...
The free-energy landscape of a small protein, the FBP 28 WW domain, has been explored using molecula...
The native state can be considered as a unique conformation of the protein molecule with the lowest ...
The free-energy landscape of a small protein, the FBP 28 WW domain, has been explored using molecula...
Herein, we present a novel Hamiltonian replica exchange protocol for classical molecular dynamics si...
The native state can be considered as a unique conformation of the protein molecule with the lowest ...
The free-energy landscape of a small protein, the FBP 28 WW domain, has been explored using molecula...
Herein, we present a novel Hamiltonian replica exchange protocol for classical molecular dynamics si...
The free-energy landscape of a small protein, the FBP 28 WW domain, has been explored using molecula...
The free-energy landscape of a small protein, the FBP 28 WW domain, has been explored using molecula...
The free-energy landscape of a small protein, the FBP 28 WW domain, has been explored using molecula...
Most proteins must fold to a well-defined structure with a minimal stability to perform their funct...
We present a theoretical framework for the study of the protein folding problem and apply it to the ...