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Coarse-grained Simulations of Biological Motors
Author(s) -
Changbong Hyeon
Publication year - 2011
Publication title -
physics and high technology
Language(s) - English
Resource type - Journals
ISSN - 1225-2336
DOI - 10.3938/phit.20.022
Subject(s) - computer science
Fig. 1. A cartoon illustrating a kinesin stepping on a microtubule track. Kinesin has two motor domains (two brown objects) to alternately bind microtubule binding sites whose affinity changes with the chemical state of nucleotide (ATP, ADP, or nucleotide free state) in the catalytic site. Tail domain extended from the motor domains is linked to a tail binding domain with which kinesins can carry cellular organelles such as vesicle, mRNA, and mitochondria along microtubules.

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