title: Mechanostability of cohesin-dockerin complexes in a structure-based model: anisotropy and lack of universality in the force profiles.
abstract: We use a structure-based coarse grained model to elucidate stretching of three cohesin-dockerin complexes that are found in the cellulosome. The average strength of mechanostability is comparable to that of the I27 domain of titin, but the force profiles depend on the pulling direction and anisotropy effects can be substantial. Even though the force profiles for individual cohesins and dockerins are similar, those for their complexes are visibly distinct for any pulling direction.
authors.affiliation: Institute of Physics, Polish Academy of Sciences, Aleja Lotników 32/46, 02-668 Warsaw, Poland.
authors.forename: Michał
authors.initials: M
authors.lastname: Wojciechowski
authors.affiliation: Materials and Surface Science Institute and Department of Physics and Energy, University of Limerick, Limerick, Ireland.
authors.forename: Damien
authors.initials: D
authors.lastname: Thompson
authors.affiliation: Institute of Physics, Polish Academy of Sciences, Aleja Lotników 32/46, 02-668 Warsaw, Poland.
authors.forename: Marek
authors.initials: M
authors.lastname: Cieplak
mesh_terms: D016880:Anisotropy; D018797:Cell Cycle Proteins / Q000737:chemistry*; D044603:Cellulosomes / Q000737:chemistry; D002868:Chromosomal Proteins, Non-Histone / Q000737:chemistry*; D064211:Connectin / Q000737:chemistry; D008956:Models, Chemical; D011485:Protein Binding; D017433:Protein Structure, Secondary; D000097722:Cohesins
chemical_list: D018797:Cell Cycle Proteins; D002868:Chromosomal Proteins, Non-Histone; D064211:Connectin; D000097722:Cohesins