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Mechanical Characterization of Motor Proteins: A Molecular Dynamics Approach

✍ Scribed by Iuliana Aprodu; Monica Soncini; Alberto Redaelli


Publisher
John Wiley and Sons
Year
2008
Tongue
English
Weight
500 KB
Volume
17
Category
Article
ISSN
1022-1344

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✦ Synopsis


Abstract

A new approach, based on molecular dynamics, is presented to measure the mechanical properties of motor proteins, which are important for accomplishing their intracellular functions. Two different set‐ups were designed to mimic the optical tweezers and surface force apparatus experiments. The results obtained show that the stiffness and elastic modulus of kinesin motor domain are 377 pN · nm^βˆ’1^ and 0.17 GPa, respectively, while the myosin motor domain is characterized by a stiffness of 271 pN · nm^βˆ’1^ and an elastic modulus of 0.26 GPa. These results suggest that the source of the very low stiffness detected for full‐length molecules is located outside of the globular part of the proteins.

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