how does the specificity change?
Homework Answers
In thrombin, the substrate specificity is very high as it cleaves only argenine-glycine bonds.
Trypsin is less specific than thrombin as it cleaves any of arg-x and lys-x bonds.
Subtillsin is least specific as it cleaves any x-x peptide bonds.
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how does the specificity change?
Substrate Specificity Example 2: Proteases Proteases - cleave peptide bonds Ami...
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...
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...
t How are donaturation and varovalo airterent a. Rydrolysis resulte to the formation of water. Hydrolysis...
t How are donaturation and varovalo airterent a. Rydrolysis resulte to the formation of water. Hydrolysis only takes place in the cytopa c. Hydrolysis results in breakingole d. Hydrolysis results in breaking ovalent bo How is folding related to function? • Folding and function are not related.. Proper folding results in propertune 0. Proper folding results in reduced un roper folding results in arratiefunct Molecules that a t folding are called a. Foldons which cellular environment is . Cytoplasm c....
Cyw Ala Ατα Ile Ausn Lou Asp aly Lys Ser Which molecule below is asubunit of...
Cyw Ala Ατα Ile Ausn Lou Asp aly Lys Ser Which molecule below is asubunit of peptide chains a. Acetic acid b. Alanine O. ATP d. Gracil Report the charge on most aqueous aspartie acid molecules at pH-7. Report the approximate p values for the amino acid whose titration curve is shown below (note there may be more slots for answer than answers). A) Value 1 B) Value 2 c) Value 3 c) Value 4 The structure of a rare...
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...
t How are donaturation and varovalo airterent a. Rydrolysis resulte to the formation of water. Hydrolysis only takes place in the cytopa c. Hydrolysis results in breakingole d. Hydrolysis results in breaking ovalent bo How is folding related to function? • Folding and function are not related.. Proper folding results in propertune 0. Proper folding results in reduced un roper folding results in arratiefunct Molecules that a t folding are called a. Foldons which cellular environment is . Cytoplasm c....
Cyw Ala Ατα Ile Ausn Lou Asp aly Lys Ser Which molecule below is asubunit of peptide chains a. Acetic acid b. Alanine O. ATP d. Gracil Report the charge on most aqueous aspartie acid molecules at pH-7. Report the approximate p values for the amino acid whose titration curve is shown below (note there may be more slots for answer than answers). A) Value 1 B) Value 2 c) Value 3 c) Value 4 The structure of a rare...
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