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🔶بیوشیمی به زبانی ساده برای مرور اساتید و دانشجویان

🔵We'll explore the fascinating world of biochemistry, from the basic principles to the latest research breakthroughs.

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2⃣.3⃣

🔘Explain the difference between a motif, fold and domain.

🔘Describe why there is a limited diversity of different protein folds.

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Bio.Ch.2.3.txt
7.9 KB
📌متن ویدئو ۲.۳
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2⃣.4⃣

🔘Describe the main #forces that determine the folding of proteins.

🔘Summarize how these forces balance in magnitude to promote #protein #folding.

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Bio.Ch.2.4.txt
6.8 KB
📌متن ویدئو ۲.۴
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2⃣.5⃣
🔘Summarize the thermodynamic hypothesis.

🔘Explain how Anfinsen's experiment supports the thermodynamic hypothesis.

🔘Explain how folding funnels are used to visualize protein folding thermodynamics.

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Bio.Ch.2.5.txt
10.8 KB
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2⃣.6⃣
🔘Explain the role of cooperativity in protein folding.

🔘Summarize the theoretical basis of Levinthal's paradox.

🔘Describe the diffusion collision and nucleation condensation models of protein folding.

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Bio.Ch.2.6.txt
9.5 KB
📌متن ویدئو۲.۶
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2⃣.7⃣
🔘Explain why there is a risk of aggregate formation for proteins folding in the cytosol.

🔘Summarize how different chaperones function to prevent protein aggregation.

🔘Explain why heat shock causes protein aggregation.

🔘Compare the chaperone function of HSP70 and HSP60.

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Bio.Ch.2.7.txt
10.3 KB
📌متن ویدئو۲.۷
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3⃣.1⃣

🔘Define reaction equilibrium

🔘Determine if a reaction is spontaneous based on the free energy of the reaction coordinates.

🔘Explain how a catalyst reduces the activation energy to speed the rate of a reaction.

🔘Understand that an enzyme stabilizes a transition state to decrease the activation energy of a reaction.

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Bio.Ch.3.1.txt
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3⃣.2⃣

🔘Recall that transient covalent bonds position the substrate in the enzyme active site to reduce the entropy of the system.

🔘Explain how weak non-covalent interactions (i.e. binding energy) reduce activation energy.

🔘Contrast Emil Fischer's lock-and-key model of enzyme specificity with the 'induced fit' hypothesis of enzyme catalysis.

🔘Define desolvation as it relates to binding energy.

#Enzyme #Catalysis

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Bio.ch.3.2.txt
8.3 KB
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3⃣.3⃣

🔘Explain why enzymes are much bigger than their respective active sites.

🔘Describe the 3-point attachment model of enzyme catalysis.

🔘Recall the role of sequential substrate binding and induced fit in enzyme catalysis. 

🔘Understand the role of phosphorylation in enzyme regulation.

♦️PLEASE NOTE: in video at 8:14, and in the slides, the charge sign is missing on the left most oxygen atom of citrate. It should appear as follows.

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Bio.Ch.3.3.txt
9.7 KB
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🔸🔸🔸🔸Software🔸🔸🔸🔸

📍PyMOL1⃣

🆙Please share it.

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📣 از مطالب کانال راضی هستین؟
public poll

بله، ولی ارسال ها کم است – 98
👍👍👍👍👍👍👍 61%

بله، بسیار عالی است – 43
👍👍👍 27%

خیر، مطالب غیر مرتبط زیاد است – 12
👍 7%

خیر ، مطالب مفید نیستند – 8
👍 5%

👥 161 people voted so far.
Pymol.1.txt
9.8 KB
📌متن ویدئو اموزش نرم افزار PyMOL قسمت اول
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3⃣.4⃣

🔘Describe regulation by post-translational proteolysis of proteins.

🔘Understand the importance of signaling peptides.  

🔘Define a zymogen. 

🔘Work through the processing of chymotrypsinogen as an example of an enzyme being regulated by post-translational proteolysis. 

🔘Work through the processing of insulin as a non-enzymatic example of regulation by post-translational proteolysis. 

#protein #processing

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3⃣.5⃣
Learning goal:

🔘Provide a detailed explanation of the blood clotting process and the role of proteolytic activation of proteins implicated in blood coagulation and hemostasis. 

Learning objectives:

🔘Paraphrase the three phases and key cellular components involved with the blood clotting process.

🔘Explain the role of proteolytic processes in the coagulation cascade and fibrin polymer formation.

🔘List the multiple functions of thrombin in the coagulation cascade.

🔘Describe inhibitory mechanisms of the coagulation cascade.

🔘Discuss the effects of too little or too much activation of the coagulation cascade on hemostasis. 

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