4) How do the binding interactions made by distant portions of a peptide substrate to chymotrypsin...
4) How do the binding interactions made by distant portions of a peptide substrate to chymotrypsin cause an increase in kcat? Assume that kcat corresponds to the chemistry step on the enzyme. 1-2 sentence answer.
Homework Answers
The binding interactions made by distant portions of a peptide substrate to chymotrypsin cause an increase in Kcat which may be due to the following reasons:
a. Remote binding can localize the substrate to the active site and position substrates relative to enzymatic functional groups.
b. They can also trigger conformational change and promote the active site environment by solvent exclusion.
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4) How do the binding interactions made by distant portions of a
peptide substrate to chymotrypsin...
Acetylcholine is the substrate for the enzyme acetylcholinesterase. 1. Suggest what sort of binding interactions could...
Acetylcholine is the substrate for the enzyme
acetylcholinesterase.
1. Suggest what sort of binding interactions could be involved
in holding acetylcholine to the active site.
2. The ester bond of acetylcholine is hydrolysed by
acetylcholinesterase. Suggest a mechanism by which the enzyme
catalyses this reaction.
3. Suggest how binding interactions might make acetylcholine
more susceptible to hydrolysis.
4. Structure I is an agonist which binds to the cholinergic
receptor and mimics the action of the natural ligand acetylcholine.
Structure II,...
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Please answer ALL questions or I'll thumbs down! 2) Imagine an enzyme that has a histidine...
Please answer ALL questions or I'll thumbs
down!
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how do you make a lineweaver-burk plot where the trend line
extends backwards? is there a way of figuring out how far back it
should extend based of your data ? As well, how do you plot two
sets of data on one graph ? Thank you! (idk if you need to see my
data-> attached below)
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Please fill in the blanks! Shown below is a proposed mechanism for the cleavage of sialic...
Please fill in the blanks!
Shown below is a proposed mechanism for the cleavage of sialic acid by the viral enzyme neuraminidase. The kcat for the wild-type enzyme at pH 6.15,37 °C is 26.8s- Y409) Y409) (D149) (D149) онон ﹀R374-1st Step -ROH R' C-N R374 (E117) (E117) +H2O ↓ 2nd Step Y409) Y409) (D149) 8 ,0149 D149) OH OH H2N R374 (E117) (E117) Part A Describe the roles of the following amino acids in the catalytic mechanism: Glul17, Tyr409, and...
biochemistry if you could please help me answer the following questions! 741) (5 pts) Transition state theory relate...
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biochemistry if you could please help me answer the following questions! * 1. (5 pts) Which...
biochemistry
if you could please help me answer the following questions!
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Acetylcholine is the substrate for the enzyme
acetylcholinesterase.
1. Suggest what sort of binding interactions could be involved
in holding acetylcholine to the active site.
2. The ester bond of acetylcholine is hydrolysed by
acetylcholinesterase. Suggest a mechanism by which the enzyme
catalyses this reaction.
3. Suggest how binding interactions might make acetylcholine
more susceptible to hydrolysis.
4. Structure I is an agonist which binds to the cholinergic
receptor and mimics the action of the natural ligand acetylcholine.
Structure II,...
Please answer ALL questions or I'll thumbs
down!
2) Imagine an enzyme that has a histidine in the substrate binding pocket that regulates substrate binding based on its protonation state to control enzyme function. Substrates can only bind in the unprotonated state; in other words, substrate binding is blocked when the histidine is protonated and when the substrate is bound, the histidine cannot be protonated. This enzyme exhibits classical Michaelis-Menten behavior. a) Assume that the pka of the histidine in...
how do you make a lineweaver-burk plot where the trend line
extends backwards? is there a way of figuring out how far back it
should extend based of your data ? As well, how do you plot two
sets of data on one graph ? Thank you! (idk if you need to see my
data-> attached below)
Biochemistry Enzyme Kinetics Assignment Four answers for this assignment will be completed in elearn: En in elearn: Enzyme Kinetics Quiz ots but must...
6. What does a buffer do? Why are bicarbonate and phosph Henderson Hasselbalch equation to calculate pH if pKa i ate really good biological buffers? Use the s 4.0, [A-1-10μΜ, and [HA-1000μΜ 7. In what eukaryotic cell structure (cytosol, nucleus, mitochondrion, inner mitochondrial membrane, rough ER, smooth ER, plasma membrane etc.) do the following functions take place? Transcription Translation (2 sites) Glycolysis Kreb's Cycle Electron transport chain AG, of a reaction is +11,600 The standard J/mol. What is K at...
Please fill in the blanks!
Shown below is a proposed mechanism for the cleavage of sialic acid by the viral enzyme neuraminidase. The kcat for the wild-type enzyme at pH 6.15,37 °C is 26.8s- Y409) Y409) (D149) (D149) онон ﹀R374-1st Step -ROH R' C-N R374 (E117) (E117) +H2O ↓ 2nd Step Y409) Y409) (D149) 8 ,0149 D149) OH OH H2N R374 (E117) (E117) Part A Describe the roles of the following amino acids in the catalytic mechanism: Glul17, Tyr409, and...
biochemistry
if you could please help me answer the following questions!
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biochemistry
if you could please help me answer the following questions!
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