WASHINGTON: Rice University researchers are modeling the movement of motor proteins along a microtubule by breaking the pathway down into its basic elements.
The study suggests that the collective behavior of motor proteins like kinesins keeps cellular transport systems robust by favoring slow and steady over maximum movement.
The interactions once thought to be of little relevance are worthy of further study, according to Rice theoretical biophysicist Anatoly Kolomeisky. Small changes that may be controlled with medications can have a large effect on cell dynamics, an important consideration in treating disease, he said.
His group’s paper in the Journal of Physics A: Mathematical and Theoretical describes a new theoretical approach to study the effect of intermolecular interactions on the dynamics of motor proteins that move along cytoskeletal filaments known as microtubules.
Motor proteins powered by adenosine triphosphate, which supplies chemical energy, “walk” along microtubules to deliver cargo throughout cells and discard trash. Previous work by Kolomeisky and his students showed how microtubules are continually built, destroyed and rebuilt by cells that reuse the molecular building blocks like Legos.
The new mathematical model built by lead author Hamid Telmouri and co-author Kareem Mehrabiani, both Rice graduate students, analyzes short sequences of those blocks to demonstrate that both strong and weak interactions are important to regulate the flux, or movement, of motor proteins.
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