Coupling of Two Motor Proteins: a New Motor Can Move Faster
arXiv:cond-mat/0502474 · doi:10.1103/PhysRevLett.94.238101
Abstract
We study the effect of a coupling between two motor domains in highly-processive motor protein complexes. A simple stochastic discrete model, in which the two parts of the protein molecule interact through some energy potential, is presented. The exact analytical solutions for the dynamic properties of the combined motor species, such as the velocity and dispersion, are derived in terms of the properties of free individual motor domains and the interaction potential. It is shown that the coupling between the motor domains can create a more efficient motor protein that can move faster than individual particles. The results are applied to analyze the motion of helicase RecBCD molecules.
References in corpus (3)
Cited by in corpus (16)
- Non-equilibrium statistical mechanics: From a paradigmatic model to biological transport
- Mechanical coupling in flashing ratchets
- Helicase processivity and not the unwinding velocity exhibits universal increase with force
- Cargo transport by several motors
- Transport of organelles by elastically coupled motor proteins
- Velocity and processivity of helicase unwinding of double-stranded nucleic acids
- Simplification of the tug-of-war model for cellular transport in cells
- Dynamic Properties of Motor Proteins with Two Subunits
- Dynamic Phase Transitions in Coupled Motor Proteins
- Interacting molecular motors: Efficiency and work fluctuations
- Force generation in small ensembles of Brownian motors
- Transport of Molecular Motor Dimers in Burnt-Bridge Models
- Interaction Between Motor Domains Can Explain the Complex Dynamics of Heterodimeric Kinesins
- Interacting Particles in Disordered Flashing Ratchets
- Resource Letter: Bio-molecular Nano-machines: where Physics, Chemistry, Biology and Technology meet
- Two Heads Are (Sometimes) Better Than One: How Rate Formulations Impact Molecular Motor Dynamics