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The
following questions are based on the papin mechanism below:
Explain the role of each amino...
The following questions are based on the papin mechanism below: Explain the role of each amino acid in the catalytic triad. Site directed mutagenesis replacing the active site asp in the papain protea...
The
following questions are based on the papin mechanism below:
Explain the role of each amino acid in the catalytic triad.
Site directed mutagenesis replacing the active site asp in the
papain protease with an ala showed that catalytic activity was not
significantly affected. Why would you think that asp is not so
critical in the cysteine proteases?
Hi R CH2 NH-R oe 0 hole oxyanion hole 0 oxyanion hole CH a)
Hi R CH2 NH-R oe 0 hole oxyanion...
5. Based on your understanding of the mechanism of proteases A. the figure below shows a part of the active sit...
5. Based on your understanding of the mechanism of proteases A. the figure below shows a part of the active site of the enzyme chymotrypsin. what are the identities of amino acids x and Y and what is this particular type of spatial arrangement of amino acids called? Alkoxide on X ? B. from the strucutres shown below, identify the two that represent the first and the second tetrahedral intermediates in the chymotrypsin catalyzed reaction. what type of attack and...
1- Hydrogen bonding between the two antiparallel strands of protein fragments described below; also show structural...
1- Hydrogen bonding between the two antiparallel strands of protein fragments described below; also show structural and spatial details ( including the correct stereochemistry for an L-amino acid) of the specific “R” groups corresponding to the amino acids specified: -NH-Gly-Phe-Ser-Ala-CO- & -CO-Tyr-Gly-Arg-Met-NH- 2- Provide a mechanistic explanation detailing how the catalytic triad of serine, histidine and aspartic acid, found in the active site site of the enzyme chymotrypsin, facilitates peptide hydrolysis. Clarify the role played by each of these amino...
24. Explain the energetic benefits of making the enzyme active state rather than to the substrate...
24. Explain the energetic benefits of making the enzyme active state rather than to the substrate conformation. Also explain how contribute to enzyme action. In other words, how do these weak intera enzyme and the transition state lower the activation energy?) of making the enzyme active site complementary to the transition nation. Also explain how multiple weak interactions words, how do these weak interactions between the 25. 1/F. The pk's of titratable groups of amino acids remain constant irrespective of...
A. Choose anly one correcet answer for each of the following questions (4 pts cach). AL Some and ...
A. Choose anly one correcet answer for each of the following questions (4 pts cach). AL Some and KM values are shown below for enzyme-substrate pairs. Which of the following enzymes is most efficient in converting the substrate into the product? b) kes.-4x10s s", KM-0.026 M d)k,,-5.7 x1o's", K-2x10s M c)人at-900 s", KM-2.5 × 10.5 M A2. Which of the following enzyme reaction mechanisms has multiple substrates? a) induced-fit e) Michaclis-Menton b) random sequential d) reversible covalent modification e) None...
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...
The
following questions are based on the papin mechanism below:
Explain the role of each amino acid in the catalytic triad.
Site directed mutagenesis replacing the active site asp in the
papain protease with an ala showed that catalytic activity was not
significantly affected. Why would you think that asp is not so
critical in the cysteine proteases?
Hi R CH2 NH-R oe 0 hole oxyanion hole 0 oxyanion hole CH a)
Hi R CH2 NH-R oe 0 hole oxyanion...
5. Based on your understanding of the mechanism of proteases A. the figure below shows a part of the active site of the enzyme chymotrypsin. what are the identities of amino acids x and Y and what is this particular type of spatial arrangement of amino acids called? Alkoxide on X ? B. from the strucutres shown below, identify the two that represent the first and the second tetrahedral intermediates in the chymotrypsin catalyzed reaction. what type of attack and...
24. Explain the energetic benefits of making the enzyme active state rather than to the substrate conformation. Also explain how contribute to enzyme action. In other words, how do these weak intera enzyme and the transition state lower the activation energy?) of making the enzyme active site complementary to the transition nation. Also explain how multiple weak interactions words, how do these weak interactions between the 25. 1/F. The pk's of titratable groups of amino acids remain constant irrespective of...
A. Choose anly one correcet answer for each of the following questions (4 pts cach). AL Some and KM values are shown below for enzyme-substrate pairs. Which of the following enzymes is most efficient in converting the substrate into the product? b) kes.-4x10s s", KM-0.026 M d)k,,-5.7 x1o's", K-2x10s M c)人at-900 s", KM-2.5 × 10.5 M A2. Which of the following enzyme reaction mechanisms has multiple substrates? a) induced-fit e) Michaclis-Menton b) random sequential d) reversible covalent modification e) None...
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...
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