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@mm.ahmed52: 🌫️🤎#foryou #sylhet
M🍫
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Sunday 06 July 2025 19:15:23 GMT
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🥂M u Nn i 🫀Ka j oL 🍅 :
🙂😅
2025-07-11 03:17:40
1
N🤴👸me❤️💌 :
🥀🥀🥀
2025-07-07 05:00:00
1
🤲নামাজ বেহেশতের চাবি 🤲 :
🤲🤲🤲
2025-07-20 09:20:54
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AK HI :
cpn ta daw
2025-07-09 09:42:53
1
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are you the (+) end of a microtubule, because i always wanna be walking towards you 🎥 Erik Schäffer Lab "Motile kinesins are motor proteins that move unidirectionally along microtubules as they hydrolyze ATP. They share a conserved motor domain (head) which harbors both the ATP- and microtubule-binding activities. The kinesin that has been studied most moves toward the microtubule (+)-end by alternately advancing its two heads along a single protofilament. This kinesin is the subject of this review. Its movement is associated to alternate conformations of a peptide, the neck linker, at the C-terminal end of the motor domain. Recent progress in the understanding of its structural mechanism has been made possible by high-resolution studies, by cryo electron microscopy and X-ray crystallography, of complexes of the motor domain with its track protein, tubulin. These studies clarified the structural changes that occur as ATP binds to a nucleotide-free microtubule-bound kinesin, initiating each mechanical step. As ATP binds to a head, it triggers orientation changes in three rigid motor subdomains, leading the neck linker to dock onto the motor core, which directs the other head toward the microtubule (+)-end. The relationship between neck linker docking and the orientations of the motor subdomains also accounts for kinesin's processivity, which is remarkable as this motor protein only falls off from a microtubule after taking about a hundred steps. As tools are now available to determine high-resolution structures of motor domains complexed to their track protein, it should become possible to extend these studies to other kinesins and relate their sequence variations to their diverse properties." #biochem #biochemistrymajor #kinesin #motorprotein #microtubule #cellbiology
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