@wjzp: أُحِبُّ الصَالِحين ولَستُ مِنهُم 💚 #السيد_السيستاني #السيد_الشيرازي #الحوزة_العلمية #شيعه_الامام_علي #السيد_محمد_رضا_الشيرازي #السيد_الخوئي #ياعلي #النجف_الأشرف

Faisal
Faisal
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Region: KW
Sunday 01 December 2024 12:46:09 GMT
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abdalla7051
abdalla :
thanks 👍
2024-12-04 01:07:24
0
tg.kd
ابــو دمــدم☫ :
محمد الصدر لم يذكر💔 দিন কারণ আমিয়েছেঅ্ফেরত দিন কা আকারণ আমিকারণ আমিফেরত দিন কারণ আমিয়েছেঅ্ফ
2024-12-01 21:21:38
64
s82x1
صوفي :
السيد محمد محمد الصدر 💔
2024-12-02 13:03:47
10
user4006147737152
וࡋߺݏࡉו𐬠ܒ߲ߺࡅ࡙ߺ :
والله مضلوم مولاي الصدر✨❤️
2024-12-02 21:47:06
10
u_bv8
『 |˹ مـٰنتظـَٰࢪ - 』 :
اين السيد الشهيد محمد الصدر 💔😔
2024-12-03 12:01:34
11
g1.me1
آحًـمًد|| :
فضائل الامام علي ع قال الامام علي (ع) (1)من لا يعرف الخير من الشر يجهل نفسه (2)من كتم سره كانت الخيرة في يده (3)من يزرع معروف يحصد الموادة
2024-12-01 22:32:30
10
user66951674018634
وعد :
اخذته عادي
2024-12-01 16:48:34
0
sabur_ruqayah313
صبر رقية | 313 :
تسمح لي اخذ الفيديو؟
2024-12-01 12:54:06
1
a_m_a_h313
شيعة حجة الله ٣١٣💚🏴 :
أحسنت يا اخي في الإسلام وابن عمي في النسب
2024-12-01 14:20:06
2
fgaur_
ذِآء. :
ولست منهم 😔
2024-12-03 19:46:10
4
ali.max21
-Ali- :
خوية ابريني ذمة خذيت فيديو
2024-12-03 19:27:46
1
sohiram
sohiram :
احب الطالحين وانا منهم
2024-12-02 17:11:14
1
x92cx_
x92cx_ :
اللهم صل على محمد وآل محمد
2024-12-01 12:48:21
2
user419026232370144
ابو كنعان :
يارب العالمين بحق محمد وآل محمد امنحني صلاحا
2024-12-01 19:15:12
1
aliwaleedjawad
أيهم الشيخ/✨ :
ليش محمد الصدر ماذكرته😭😭
2024-12-02 16:38:25
0
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are you the (+) end of a microtubule, because i always wanna be walking towards you 🎥 Erik Schäffer Lab
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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