@article{
 title = {Mechanical catalysis on the centimeter scale},
 type = {article},
 year = {2015},
 identifiers = {[object Object]},
 keywords = {Autocatalysis,Conformation change,Enzyme,Inhibitor,Magnetic catalysis,Reaction phase},
 volume = {12},
 id = {a293d266-1809-3b1c-8081-84aecf603699},
 created = {2016-04-10T08:08:11.000Z},
 file_attached = {false},
 profile_id = {930c6fc3-4f7d-3268-8cb7-e7bbdd7b5ce3},
 last_modified = {2017-03-15T15:23:23.867Z},
 read = {true},
 starred = {false},
 authored = {true},
 confirmed = {false},
 hidden = {false},
 private_publication = {false},
 abstract = {© 2015 The Author(s) Published by the Royal Society. All rights reserved. Enzymes play important roles in catalysing biochemical transaction paths, acting as logical machines through the morphology of the processes. A key challenge in elucidating the nature of these systems, and for engineering manufacturing methods inspired by biochemical reactions, is to attain a comprehensive understanding of the stereochemical ground rules of enzymatic reactions. Here, we present a model of catalysis that can be performed magnetically by centimetre-sized passive floating units. The designed system, which is equipped with permanent magnets only, passively obeys the local causalities imposed by magnetic interactions, albeit it shows a spatial behaviour and an energy profile analogous to those of biochemical enzymes. In this process, the enzyme units trigger physical conformation changes of the target by levelling out the magnetic potential barrier (activation potential) to a funnel type and, thus, induce cascading conformation changes of the targeted substrate units reacting in parallel. The inhibitor units, conversely, suppress such changes by increasing the potential. Because the model is purely mechanical and established on a physics basis in the absence of turbulence, each performance can be explained by the morphology of the unit, extending the definition of catalysis to systems of alternative scales.},
 bibtype = {article},
 author = {Miyashita, S. and Audretsch, C. and Nagy, Z. and Füchslin, R.M. and Pfeifer, R.},
 journal = {Journal of the Royal Society Interface},
 number = {104}
}

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All rights reserved. Enzymes play important roles in catalysing biochemical transaction paths, acting as logical machines through the morphology of the processes. A key challenge in elucidating the nature of these systems, and for engineering manufacturing methods inspired by biochemical reactions, is to attain a comprehensive understanding of the stereochemical ground rules of enzymatic reactions. Here, we present a model of catalysis that can be performed magnetically by centimetre-sized passive floating units. The designed system, which is equipped with permanent magnets only, passively obeys the local causalities imposed by magnetic interactions, albeit it shows a spatial behaviour and an energy profile analogous to those of biochemical enzymes. In this process, the enzyme units trigger physical conformation changes of the target by levelling out the magnetic potential barrier (activation potential) to a funnel type and, thus, induce cascading conformation changes of the targeted substrate units reacting in parallel. The inhibitor units, conversely, suppress such changes by increasing the potential. Because the model is purely mechanical and established on a physics basis in the absence of turbulence, each performance can be explained by the morphology of the unit, extending the definition of catalysis to systems of alternative scales.","bibtype":"article","author":"Miyashita, S. and Audretsch, C. and Nagy, Z. and Füchslin, R.M. and Pfeifer, R.","journal":"Journal of the Royal Society Interface","number":"104","bibtex":"@article{\n title = {Mechanical catalysis on the centimeter scale},\n type = {article},\n year = {2015},\n identifiers = {[object Object]},\n keywords = {Autocatalysis,Conformation change,Enzyme,Inhibitor,Magnetic catalysis,Reaction phase},\n volume = {12},\n id = {a293d266-1809-3b1c-8081-84aecf603699},\n created = {2016-04-10T08:08:11.000Z},\n file_attached = {false},\n profile_id = {930c6fc3-4f7d-3268-8cb7-e7bbdd7b5ce3},\n last_modified = {2017-03-15T15:23:23.867Z},\n read = {true},\n starred = {false},\n authored = {true},\n confirmed = {false},\n hidden = {false},\n private_publication = {false},\n abstract = {© 2015 The Author(s) Published by the Royal Society. 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