The Effect of Different Force Applications on the Protein-Protein Complex Barnase-Barstar
AUTOR(ES)
Neumann, Jan
FONTE
The Biophysical Society
RESUMO
Steered molecular dynamics simulations are a tool to examine the energy landscape of protein-protein complexes by applying external forces. Here, we analyze the influence of the velocity and geometry of the probing forces on a protein complex using this tool. With steered molecular dynamics, we probe the stability of the protein-protein complex Barnase-Barstar. The individual proteins are mechanically labile. The Barnase-Barstar binding site is more stable than the folds of the individual proteins. By using different force protocols, we observe a variety of responses of the system to the applied tension.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=2741585Documentos Relacionados
- Protein-protein interaction: a genetic selection for compensating mutations at the barnase-barstar interface.
- Protein-protein interactions in the synaptonemal complex.
- Protein-protein interactions in the rigor actomyosin complex.
- Effect of the ion-protein dispersion interactions on the protein-surface and protein-protein interactions
- Mapping of protein-protein interactions within the DNA-dependent protein kinase complex.