The effect of different force applications on the protein-protein complex Barnase-Barstar.
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.
Neumann
Jan
J
Angewandte Physik und Biophysik, Ludwig-Maximilians Universität, Munich, Germany.
Gottschalk
Kay-Eberhard
KE
D001426:Bacterial Proteins / Q000737:chemistry / Q000378:metabolism*; D001696:Biomechanical Phenomena; D007700:Kinetics; D008958:Models, Molecular; D011485:Protein Binding; D011487:Protein Conformation; D011489:Protein Denaturation; D055550:Protein Stability; D012260:Ribonucleases / Q000737:chemistry / Q000378:metabolism*; D014783:Viscosity
D001426:Bacterial Proteins; C057438:barstar protein, Bacillus amyloliquefaciens; D012260:Ribonucleases; C019760:Bacillus amyloliquefaciens ribonuclease