🎥یک ویدیوی فوقالعاده از آنزیم DNA gyrase مشغول کار, و به دنبال اون هم انزیم پلیمراز رو میبینیم که مشغول همانند سازی هست

Dna gyrase at work to uncoil a dna double helix

🎞Dna gyrase
آنزیم باز کننده و ریلکس کننده ی DNA
🎞Uncoil
باز کردن درهم پیچدگی
🎞Double helix
مارپیچ دو رشته ای

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📌متن ویدئو ۲.۱
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2⃣.2⃣

🔘Label the atoms and bonds in a polypeptide.

🔘Recognize the unique properties of each of the bonds in a polypeptide chain.

🔘Describe a Ramachandran plot and how it is generated.

🔘Identify the three secondary structures of proteins.

🔘Predict the secondary structure of a polypeptide based on its phi and psi angles.

🔘Explain how hydrogen bonding contributes to the formation of secondary structure.

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📌متن ویدئو ۲.۲
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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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📌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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📌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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📌متن ویدئو۲.۵
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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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📌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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📌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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📌متن ویدئو۳.۱
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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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📌متن ویدئو۳.۲
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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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📌متن ویدئو۳.۳
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