title: Protein unfolding under force: crack propagation in a network.
abstract: The mechanical unfolding of a set of 12 proteins with diverse topologies is investigated using an all-atom constraint-based model. Proteins are represented as polypeptides cross-linked by hydrogen bonds, salt bridges, and hydrophobic contacts, each modeled as a harmonic inequality constraint capable of supporting a finite load before breaking. Stereochemically acceptable unfolding pathways are generated by minimally overloading the network in an iterative fashion, analogous to crack propagation in solids. By comparing the pathways to those from molecular dynamics simulations and intermediates identified from experiment, it is demonstrated that the dominant unfolding pathways for 9 of the 12 proteins studied are well described by crack propagation in a network.
authors.affiliation: Department of Physics and Center for Biological Physics, Arizona State University, Tempe, Arizona, USA.
authors.forename: Adam M R
authors.initials: AM
authors.lastname: de Graff
authors.forename: Gareth
authors.initials: G
authors.lastname: Shannon
authors.forename: Daniel W
authors.initials: DW
authors.lastname: Farrell
authors.forename: Philip M
authors.initials: PM
authors.lastname: Williams
authors.forename: M F
authors.initials: MF
authors.lastname: Thorpe
mesh_terms: D001696:Biomechanical Phenomena; D004548:Elasticity; D006860:Hydrogen Bonding; D055595:Mechanical Phenomena; D056004:Molecular Dynamics Simulation; D011487:Protein Conformation; D058767:Protein Unfolding; D011506:Proteins / Q000737:chemistry*; D013314:Stress, Mechanical
chemical_list: D011506:Proteins