منابع مشابه
Nonequilibrium Energetics of Molecular Motor Kinesin
Molecular motors are nonequilibrium open systems that convert chemical energy to mechanical work. Here we investigate the nonequilibrium energetics of a single molecule kinesin by measuring the motion of an attached probe particle and its response to external forces with optical tweezers. The sum of the heat dissipation estimated from the violation of the fluctuation-response relation and the o...
متن کاملInsight into the molecular mechanism of the multitasking kinesin-8 motor.
Members of the kinesin-8 motor class have the remarkable ability to both walk towards microtubule plus-ends and depolymerise these ends on arrival, thereby regulating microtubule length. To analyse how kinesin-8 multitasks, we studied the structure and function of the kinesin-8 motor domain. We determined the first crystal structure of a kinesin-8 and used cryo-electron microscopy to calculate ...
متن کاملMotor proteins of the kinesin superfamily: structure and mechanism.
Kinesins are ATP-driven microtubule motor proteins that produce directed force. The kinesin superfamily currently encompasses over 100 eukaryotic proteins containing a common motor domain. Both the nucleotide-binding fold and active-site chemistry of the motor domain are also present in the actin-based motor, myosin. Kinesins can be classified into three groups based on the position of their mo...
متن کاملMolecular phylogeny of the kinesin family of microtubule motor proteins.
The rapidly expanding kinesin family of microtubule motor proteins includes proteins that are involved in diverse microtubule-based functions in the cell. Phylogenetic analysis of the motor regions of the kinesin proteins reveals at least five clearly defined groups that are likely to identify kinesins with different roles in basic cellular processes. Two of the groups are consistent with overa...
متن کاملKinesin: switch I & II and the motor mechanism.
New crystal structures of the kinesin motors differ from previously described motor-ADP atomic models, showing striking changes both in the switch I region near the nucleotide-binding cleft and in the switch II or 'relay' helix at the filament-binding face of the motor. The switch I region, present as a short helix flanked by two loops in previous motor-ADP structures, rearranges into a pseudo-...
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ژورنال
عنوان ژورنال: Seibutsu Butsuri
سال: 2002
ISSN: 0582-4052,1347-4219
DOI: 10.2142/biophys.42.156