2) Trypsin and Chymotrypsin are enzymes belonging to the serine protease family. These enzymes cleave specific amino acids at the C-terminus of the peptide bond. a) After which ends does chymotrypsin break down? b) After which ends does trypsin cleave? c) How many peptides are formed as a result of the breakdown of a protein with the amino acid sequence given below by trypsin? d) How many peptides are formed as a result of the breakdown of a protein with the amino acid sequence given below by chymotrypsin? e) How many peptides are formed as a result of the breakdown of a protein with the amino acid sequence given below by trypsin and chymotrypsin? The amino acid sequence of the myoglobin protein: MGLSDGEWQLVLNVWGKVEADIPGHGQEVLIRLFKGHPETLEKFDKFKHLKSEDEMKASE DLKKHGATVLTALGGILKKKGHHEAEIKPLAQSHATKHKIPVKYLEFISECIIQVLQSKH PGDFGADAQGAMNKALELFRKDMASNYKELGFQG
Added by Jonathan K.
Step 1
**Step 2:** Trypsin cleaves peptide bonds after positively charged amino acids such as lysine and arginine. **Step 3:** To determine the number of peptides formed by trypsin breakdown of the myoglobin protein, we need to identify the cleavage sites. The amino Show more…
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Below is the catalytic mechanism of Trypsin, a protease often used in biochemistry to cut proteins into fragments for analysis. Please identify the method(s) of catalysis used in each step of Trypsin's mechanism. Provide a one-sentence rationale for your identification. Trypsin, Chymotrypsin, and Elastase are homologous proteases; they perform the same function using conserved active site residues. Despite their similar enzyme mechanisms, they each have a different set of substrates. Trypsin cleaves peptide bonds between Lys or Arg; Chymotrypsin cleaves peptides bond between large, bulky amino acids; Elastase cleaved peptide bonds between small, uncharged amino acids. In a 2-3 sentences, hypothesize why these three enzymes only act of certain substrates despite performing essentially the same function and by the same mechanism.
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Question 1: You have purified a new peptide hormone. To determine its amino acid sequence, you have digested the polypeptide with trypsin and, in a separate reaction, you have digested the polypeptide with chymotrypsin. Cleavage with trypsin yielded 5 peptides that were sequenced by Edman degradation, as shown in the following: KGE NAIIK NAYK SQTPLVLFK YGGFMTSEK Cleavage with chymotrypsin yielded 4 peptides that were sequenced by Edman degradation: KKGE YGGF KNAIIKNAY MTSEKSQTPLVLF a) What is the N-terminal amino acid of the protein? b) What chemical reagents can you use to identify the N-terminus of a protein/peptide? What other amino acids in the peptide will react with that reagent?
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Proteins are made of amino acids linked together into a(n) ___?___. Amino acids are linked together by forming a(n)___?___ between the ___?___ group of one amino acid with the ___?___ group of another amino acid. This means that proteins have structural polarity, meaning one end is different from the other end. The start of a protein is called the ___?___ while the end is called the ___?___. The ___?___ gives each amino acid its distinct chemical properties. The linear sequence of amino acids determines a protein's ___?___, or folded, 3-dimensional structure. WORD TABLE: side chain polypeptide chain hydrogen bond amino peptide bond enzyme conformation N-terminus 3' end 5' end phosphate carboxyl chaperone C-terminus sulfate denatured
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