title: The mechanical unfolding of ubiquitin through all-atom Monte Carlo simulation with a Go-type potential.
abstract: The mechanical unfolding of proteins under a stretching force has an important role in living systems and is a logical extension of the more general protein folding problem. Recent advances in experimental methodology have allowed the stretching of single molecules, thus rendering this process ripe for computational study. We use all-atom Monte Carlo simulation with a Gō-type potential to study the mechanical unfolding pathway of ubiquitin. A detailed, robust, well-defined pathway is found, confirming existing results in this vein though using a different model. Additionally, we identify the protein's fundamental stabilizing secondary structure interactions in the presence of a stretching force and show that this fundamental stabilizing role does not persist in the absence of mechanical stress. The apparent success of simulation methods in studying ubiquitin's mechanical unfolding pathway indicates their potential usefulness for future study of the stretching of other proteins and the relationship between protein structure and the response to mechanical deformation.
authors.affiliation: Department of Chemistry and Chemical Biology, Harvard University, Cambridge, Massachusetts, USA.
authors.forename: Ariel
authors.initials: A
authors.lastname: Kleiner
authors.forename: Eugene
authors.initials: E
authors.lastname: Shakhnovich
mesh_terms: D003198:Computer Simulation; D008956:Models, Chemical; D008958:Models, Molecular; D015233:Models, Statistical; D009010:Monte Carlo Method; D009038:Motion; D011487:Protein Conformation; D011489:Protein Denaturation; D017510:Protein Folding; D025801:Ubiquitin / Q000737:chemistry* / Q000648:ultrastructure*
chemical_list: D025801:Ubiquitin