--- res: bibo_abstract: - In the living cell, we encounter a large variety of motile processes such as organelle transport and cytoskeleton remodeling. These processes are driven by motor proteins that generate force by transducing chemical free energy into mechanical work. In many cases, the molecular motors work in teams to collectively generate larger forces. Recent optical trapping experiments on small teams of cytoskeletal motors indicated that the collectively generated force increases with the size of the motor team but that this increase depends on the motor type and on whether the motors are studied in vitro or in vivo. Here, we use the theory of stochastic processes to describe the motion of N motors in a stationary optical trap and to compute the N-dependence of the collectively generated forces. We consider six distinct motor types, two kinesins, two dyneins, and two myosins. We show that the force increases always linearly with N but with a prefactor that depends on the performance of the single motor. Surprisingly, this prefactor increases for weaker motors with a lower stall force. This counter-intuitive behavior reflects the increased probability with which stronger motors detach from the filament during strain generation. Our theoretical results are in quantitative agreement with experimental data on small teams of kinesin-1 motors.@eng bibo_authorlist: - foaf_Person: foaf_givenName: Mehmet C foaf_name: Ucar, Mehmet C foaf_surname: Ucar foaf_workInfoHomepage: http://www.librecat.org/personId=50B2A802-6007-11E9-A42B-EB23E6697425 orcid: 0000-0003-0506-4217 - foaf_Person: foaf_givenName: Reinhard foaf_name: Lipowsky, Reinhard foaf_surname: Lipowsky bibo_doi: 10.1021/acs.nanolett.9b04445 bibo_issue: '1' bibo_volume: 20 dct_date: 2020^xs_gYear dct_identifier: - UT:000507151600087 dct_isPartOf: - http://id.crossref.org/issn/1530-6984 - http://id.crossref.org/issn/1530-6992 dct_language: eng dct_publisher: American Chemical Society@ dct_title: Collective force generation by molecular motors is determined by strain-induced unbinding@ fabio_hasPubmedId: '31797672' ...