Reconstructing the free-energy landscape associated to molecular motors processivity.
We propose a biochemical model providing the kinetic and energetic descriptions of the processivity dynamics of kinesin and dinein molecular motors. Our approach is a modified version of a well known model describing kinesin dynamics and considers the presence of a competitive inhibition reaction by ADP. We first reconstruct a continuous free-energy landscape of the cycle catalyst process that allows us to calculate the number of steps given by a single molecular motor. Then, we calculate an analytical expression associated to the translational velocity and the stopping time of the molecular motor in terms of time and ATP concentration. An energetic interpretation of motor processivity is discussed in quantitative form by using experimental data. We also predict a time duration of collective processes that agrees with experimental reports.
Facultad de Ciencias, Universidad Nacional Autónoma de México, Circuito exterior de Ciudad Universitaria, México Distrito Federal 04530, Mexico. surfsk8.jared@gmail.com
Nazul Jared
NJ
López Alamilla
Ivan
I
Santamaría Holek
D000244:Adenosine Diphosphate / Q000737:chemistry / Q000378:metabolism; D055162:Biocatalysis; D016547:Kinesins / Q000037:antagonists & inhibitors / Q000378:metabolism; D007700:Kinetics; D008958:Models, Molecular; D020409:Molecular Motor Proteins / Q000037:antagonists & inhibitors / Q000378:metabolism*; D014176:Protein Biosynthesis; D013816:Thermodynamics
D020409:Molecular Motor Proteins; D000244:Adenosine Diphosphate; D016547:Kinesins