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Published on: November 26, 2019
Molecular Active Matter, Kinetic Asymmetry, and Non-Reciprocal Interactions
Niladri Sekhar Mandal1,2, Xiaotian Lu1, Ayusman Sen1,3
1Department of Chemical Engineering, The Pennsylvania State University, University Park, Pennsylvania, USA.
Molecular enzymes exhibit directional motion through kinetic and diffusion asymmetry, generating complex outputs from simple energy inputs. This explains enzyme chemotaxis and interactions, potentially leading to life's fundamental properties.
Area of Science:
- Biophysics
- Chemical Engineering
- Materials Science
Background:
- Active matter research often draws analogies between molecular and macroscopic scales, leading to confusion regarding driving forces.
- Distinguishing between phoretic and hydrodynamic forces is crucial for understanding molecular active matter.
Purpose of the Study:
- To elucidate the fundamental mechanisms driving directional motion in nanoscale enzymes.
- To develop a model explaining chemotaxis and inter-enzyme interactions at the molecular level.
Main Methods:
- Theoretical modeling combining kinetic asymmetry, diffusion asymmetry, and dissipation.
- Analysis of symmetry breaking principles at the nanoscale.
Main Results:
- A model demonstrating how asymmetry and dissipation enable directional motion in molecular enzymes.
- Explanation of both positive and negative chemotaxis in molecular catalysts.
- Emergence of non-reciprocal interactions between enzymes sharing substrates/products.
Conclusions:
- The proposed mechanism provides a unified framework for understanding molecular active matter.
- Non-reciprocal interactions at the molecular scale may be key to emergent properties like memory and order.
- These emergent properties are fundamental to the transition from non-living matter to life.
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