منابع مشابه
Overdamped mechanical model of myosin II
Due to their small size molecular systems are often overdamped and they are affected by significant fluctuations due to thermal forces. In this paper we investigate the effect of overdamping on a simple mechanical model of myosin II, the motor protein responsible for muscle contraction. We demonstrate that this model, based on the experimentally observed shape of the protein’s subdomains, is co...
متن کاملA mechanical function of myosin II in cell motility.
Myosin II mutant Dictyostelium amoebae crawl more slowly than wild-type cells. Thus, myosin II must contribute to amoeboid locomotion. We propose that contractile forces generated by myosin II help the cell's rear edge to detach from the substratum and retract, allowing the cell to continue forward. To test this hypothesis, we measured the speed of wild-type and myosin II null mutant Dictyostel...
متن کاملMechanical properties of human tooth approximated with overdamped oscillators*
Numerical calculations and analysis of the tension states in hard tissues of tooth are very interesting and important issues from the orthodontist’s point of view. Orthodontic methods of treatment can have a dramatic effect on children’s long-term dental health and facial appearance. Research done in this field shows that due to understanding mechanics of masticatory organ it is possible to att...
متن کاملSensitivity of small myosin II ensembles from different isoforms to mechanical load and ATP concentration.
Based on a detailed crossbridge model for individual myosin II motors, we systematically study the influence of mechanical load and adenosine triphosphate (ATP) concentration on small myosin II ensembles made from different isoforms. For skeletal and smooth muscle myosin II, which are often used in actomyosin gels that reconstitute cell contractility, fast forward movement is restricted to a sm...
متن کاملDictyostelium discoideum myosin II: characterization of functional myosin motor fragments.
The transient kinetic properties of the recombinant myosin head fragments M761 and M781, which both lack the light chain binding domain (LCBD) and correspond to the first 761 and 781 residues of Dictyostelium discoideum myosin II, were compared with those of the subfragment 1-like fragment M864 and a shorter catalytic domain fragment M754. The properties of M761, M781, and M864 are almost ident...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
ژورنال
عنوان ژورنال: Periodica Polytechnica Civil Engineering
سال: 2013
ISSN: 0553-6626,1587-3773
DOI: 10.3311/ppci.2137