Homework Answers
C) The substrate binding pockets accommodate different amino acids.
They both have different signatures in the loop regions, which ultimately depends on the residues in the binding pockets.
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Trypsin, chymotrypsin, and elastase are all serine proteases that cleave after different amino acids. What is...
1) (10 pts) Serine proteases are enzymes that cleave peptide bonds in proteins. Explain using words...
1) (10 pts) Serine proteases are enzymes that cleave peptide bonds in proteins. Explain using words (drawings OR both) why serine proteases cleave either before or after different amino acid residues. Talk about at least two of the following proteases: Chymotrypsin, Trypsin, or Elastase. mod 2) (10pts) Below is a hypothetical peptide sequence. Give the peptide fragments that will occur by enzymatic degradation using Trypsin and Chymotrypsin DARSKWKSENLIRTY 3) (10 pts) All superfamilies of serine proteases use the catalytic triad...
Name: 09) (5 points) Trypsin and chymotrypsin are members of the family of serine proteases -...
Name: 09) (5 points) Trypsin and chymotrypsin are members of the family of serine proteases - they cleave (cut) peptide bonds at the C-terminal end of specific residues. a) Chymotrypsin cleaves peptide bonds at the C-terminal end of what type of amino acid? b) Briefly describe the specific properties of the binding pocket in chymotrypsin that allows proper orientation of the substrate to cleave at the position you described in (a). c) Trypsin cleaves peptide bonds at the C-terminal end...
225. Describe what serine proteases are, what they do, what their active sites are like including...
225. Describe what serine proteases are, what they do, what their active sites are like including the catalytic triad and the oxyanion hole, how is specificity achieved (compare chymotrypsin, trypsin, and elastase), and what is the molecular mechanism for chymotrypsin 226. What are other types of proteases? 227. Why are proteases good drug targets ? 228. What is the enzymatic function of carbonic anhydrase? 229. What is the physiological importance of carbonic anhydrase?
What is the catalytic triad of chymotrypsin, a type of serine protease? the enzyme-cofactor-intermediate complex the...
What is the catalytic triad of chymotrypsin, a type of serine protease? the enzyme-cofactor-intermediate complex the amino acids serine, histidine, and aspartate the amino acids cysteine, histidine, and aspartate the enzyme-cofactor-substrate complex the amino acids serine, histidine, and glutamate
1.. Example questions to guide you through the mechanism study of Serine proteases Describe substrate binding,...
1.. Example questions to guide you through the mechanism study of Serine proteases Describe substrate binding, including the role and chemical nature of the "specificity pocket" in chymotrypsin, and which peptide bond in the substrate (relative to the specificity group) will be cleaved. Draw the structure of the catalytic triad at the beginning of the reaction, and explain how the states of ionization and hydrogen bonding pattern of those 3 groups change step by step during catalysis. Explain the role...
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...
1) (10 pts) Serine proteases are enzymes that cleave peptide bonds in proteins. Explain using words (drawings OR both) why serine proteases cleave either before or after different amino acid residues. Talk about at least two of the following proteases: Chymotrypsin, Trypsin, or Elastase. mod 2) (10pts) Below is a hypothetical peptide sequence. Give the peptide fragments that will occur by enzymatic degradation using Trypsin and Chymotrypsin DARSKWKSENLIRTY 3) (10 pts) All superfamilies of serine proteases use the catalytic triad...
Name: 09) (5 points) Trypsin and chymotrypsin are members of the family of serine proteases - they cleave (cut) peptide bonds at the C-terminal end of specific residues. a) Chymotrypsin cleaves peptide bonds at the C-terminal end of what type of amino acid? b) Briefly describe the specific properties of the binding pocket in chymotrypsin that allows proper orientation of the substrate to cleave at the position you described in (a). c) Trypsin cleaves peptide bonds at the C-terminal end...
225. Describe what serine proteases are, what they do, what their active sites are like including the catalytic triad and the oxyanion hole, how is specificity achieved (compare chymotrypsin, trypsin, and elastase), and what is the molecular mechanism for chymotrypsin 226. What are other types of proteases? 227. Why are proteases good drug targets ? 228. What is the enzymatic function of carbonic anhydrase? 229. What is the physiological importance of carbonic anhydrase?
What is the catalytic triad of chymotrypsin, a type of serine protease? the enzyme-cofactor-intermediate complex the amino acids serine, histidine, and aspartate the amino acids cysteine, histidine, and aspartate the enzyme-cofactor-substrate complex the amino acids serine, histidine, and glutamate
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...
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