Explain why one serine protease, trypsin, only cleaves peptides after lysine and arginine residues. Thanks!
Explain why one serine protease, trypsin, only cleaves peptides after lysine and arginine residues.
Thanks!
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Explain why one serine protease, trypsin, only cleaves peptides
after lysine and arginine residues.
Thanks!
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...
Trypsin, chymotrypsin, and elastase are all serine proteases that cleave after different amino acids. What is...
Trypsin, chymotrypsin, and elastase are all serine proteases that cleave after different amino acids. What is responsible for the substrate specificity? Choose one: A. Different amino acids involved in the catalytic triad OB. Each protease is made in a different cell type. C. The substrate binding pockets accommodate different amino acids. D. Different catalytic mechanisms
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...
1. Explain why polyaspartatic acid (a peptide containing only aspartic acid residues) does NOT form an...
1. Explain why polyaspartatic acid (a peptide containing only aspartic acid residues) does NOT form an alpha helix at pH 7.0 but can at pH 2. 6. 2. What kind of non-covalent interaction would the following pairs of amino acids have in the three dimensional structure of a protein at pH 7.0? a) His-Asp b) Tyr-Asp c) Val-Leu d) Trp-Gln 3. Explain how the difference in structure of hemoglobin and myoglobin contribute to their different functions.
Please explain, Thanks! The following image shows the 20 amino acids found in proteins. OH CH...
Please explain, Thanks!
The following image shows the 20 amino acids found in proteins. OH CH H HNCOOH Glycine HN HẠN CHO Alanine HẠN COOH Serine н соон Threonine Cysteine HAN COOHHN COOH Nлсоон н соон Methionine Valine Leucine Isoleucine Proline OOH MNCOOHHN COOH HN COOH H COOH HẠNỐIOOH Apartic Acid Phenylalanine Tyrosine Tryptophan Glutamic Acid HNCOOHH COOH Asparagine Glutamine HNCOOHNCOOH Histidine Lysine н соон Arginine Imagine that in a protein, a lysine amino acid is replaced with an isoleucine....
please explain why thanks! After cell division, daughter cells contain the same amount of DNA as...
please explain why thanks!
After cell division, daughter cells contain the same amount of DNA as in the original cell. This is due to A protein synthesis. B. recombination c pairing of homologous chromosomes. OD meiosis E DNA replication
part c only. please explain why and show clear steps. thanks! 1. For each of the...
part c only. please explain why and show clear steps.
thanks!
1. For each of the following groups G, determine whether H is a normal sub- group of G. If H is a normal subgroup, write out a Cayley table for the factor group G/H. (a) G = S4 and H = A4 (b) G = As and H = {(1), (123), (132) (c) G = S4 and H = D4 (d) G = Q8 and H = {1,-1,1, -I}...
4. In one sentence only, explain why there is a correlation between the solubility of an...
4. In one sentence only, explain why there is a correlation between the solubility of an ionic compound and the ionic strength of a solution. You may be penalized for writing more than one sentence so please be sure you answer concise and clear (4 points)
Please and thanks you.Can anyone explain me this question in detail if we use only one...
Please and thanks you.Can anyone explain me this question in detail if we use only one tree for different messages.a Huffman tree was designed using frequencies taken from a given message, and for every new message we would have to build a new tree. Imagine instead that we had built one tree to encode all different messages (in English, say). How would you determine what that Huffman tree should look like? What would be the advantages and disadvantages of building...
Explain why a mutation in only one of two copies of a proto-oncogene in a diploid...
Explain why a mutation in only one of two copies of a proto-oncogene in a diploid cell can promote the development of cancer (5 points), whereas both copies of a tumor-suppressor gene need to be mutated to do likewise (5 points).
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...
Trypsin, chymotrypsin, and elastase are all serine proteases that cleave after different amino acids. What is responsible for the substrate specificity? Choose one: A. Different amino acids involved in the catalytic triad OB. Each protease is made in a different cell type. C. The substrate binding pockets accommodate different amino acids. D. Different catalytic mechanisms
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...
Please explain, Thanks!
The following image shows the 20 amino acids found in proteins. OH CH H HNCOOH Glycine HN HẠN CHO Alanine HẠN COOH Serine н соон Threonine Cysteine HAN COOHHN COOH Nлсоон н соон Methionine Valine Leucine Isoleucine Proline OOH MNCOOHHN COOH HN COOH H COOH HẠNỐIOOH Apartic Acid Phenylalanine Tyrosine Tryptophan Glutamic Acid HNCOOHH COOH Asparagine Glutamine HNCOOHNCOOH Histidine Lysine н соон Arginine Imagine that in a protein, a lysine amino acid is replaced with an isoleucine....
please explain why thanks!
After cell division, daughter cells contain the same amount of DNA as in the original cell. This is due to A protein synthesis. B. recombination c pairing of homologous chromosomes. OD meiosis E DNA replication
part c only. please explain why and show clear steps.
thanks!
1. For each of the following groups G, determine whether H is a normal sub- group of G. If H is a normal subgroup, write out a Cayley table for the factor group G/H. (a) G = S4 and H = A4 (b) G = As and H = {(1), (123), (132) (c) G = S4 and H = D4 (d) G = Q8 and H = {1,-1,1, -I}...
4. In one sentence only, explain why there is a correlation between the solubility of an ionic compound and the ionic strength of a solution. You may be penalized for writing more than one sentence so please be sure you answer concise and clear (4 points)
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