Coupling of two motor proteins: a new motor can move faster.
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 RecBCD helicase molecules.
Stukalin
Evgeny B
EB
Department of Chemistry, Rice University, Houston, Texas 77005, USA.
Phillips
Hubert
H
Kolomeisky
Anatoly B
AB
D004247:DNA / Q000737:chemistry / Q000378:metabolism; D004265:DNA Helicases / Q000737:chemistry* / Q000378:metabolism; D043211:Exodeoxyribonuclease V / Q000737:chemistry* / Q000378:metabolism; D007700:Kinetics; D008954:Models, Biological; D008956:Models, Chemical; D017434:Protein Structure, Tertiary; D013269:Stochastic Processes
D004247:DNA; D043211:Exodeoxyribonuclease V; D004265:DNA Helicases