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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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🔘Explain the difference between a motif, fold and domain.
🔘Describe why there is a limited diversity of different protein folds.
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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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🔘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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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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🔘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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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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🔘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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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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🔘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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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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🔘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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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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🔘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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Forwarded from Biochemistry (✨Reza)
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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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🔘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.
@Medterms
@Essential_Biochemistry
Biochemistry via @vote
📣 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.
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.
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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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🔘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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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.
@Medterms
@Essential_Biochemistry