4. Show exactly which peptide bonds you would expect trypsin to cleave if you set a digest with the sample below. H3N*Gly Y Ille Yval YCys Glu Gin Ala Ser Val Pro Leu Cys Asp Arg (Lys (Phe AsnCOO- Lys Tyr Thr YLeu Y His 202
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- Draw each amino acid in its dipolar ion form. a. Thr b. Ala c. Leu d. LysHow many small peptide fragments will result if you treat the peptide Gly–Trp–Ala–Leu–Arg–Ala–Lys–Trp–Gly–Arg–Phe–His–Pro–Ala–Tyr with pepsin?1. Draw the most acidic forms of the following peptides: a. ELVIS b. LIVES c. Approximate the pI of these two peptides. d. What is the predominant form of ELVIS and LIVES at physiological pH?
- Amino acids project from each polypeptide backbone in a β-sheet in an alternating fashion (oneabove the plane and the next below the plane – see Fig 3.8B). Consider the following proteinsequence: Leu-Lys-Val-Asp-Ile-Ser-Leu-Arg-Leu-Lys-Ile-Arg-Phe-Glu.a. Is there a pattern to these amino acids? If so, what is it? b. What does this sequence of amino acids mean for the hydrophobicity/hydrophilicity of theresulting β-sheet? c. Can you make a prediction about how the β-sheet will be arranged in higher levels of protein structure? If so, what prediction would you make?1. Use the info of this molecule as well as the attached addendum to demonstrate the flow of genetic information to protein sequence as described by the so-called “Central Dogma” . Clearly indicate the direction of your polynucleotide strands and peptide/protein. ATG GCA TGC AAT AGC TCA TGC 2. What would happen to the amino acid sequence if the underlined nucleotide (C) would change to an A?Write the chemical structure of peptide containing the following amino acid PRO-SER-GLY-LEU I NEED IT ASAP PLEASE
- Draw the ff. peptides: DK YES CHEM What is the pI of each peptide? Predict the ionic form of the peptide (given above) that will predominate at: pH 1 pH 7 pH 131. Considering the following nucleotide sequence in an mRNA molecule: 5’ AUG UUA CGU AAU GCU GUC GAA UCU AUU UGC UUU ACA UAA 3' d) Write the amino acid sequence of the peptide synthesized from the given mRNA nucleotide sequence. e) Draw the structure of the pertide fragment made up of the first five (5) amino acids in the given polypeptide.2- Some proteins contain additional amino acids that arise by modification of an amino acid already present in a peptide , examples include: a) Gamma Amino Butyric Acid. b) 5 - hydroxy Lysine c) 4 - hydroxy proline d) All of the above e) None of the above
- Cholera is a disease caused by bacteria that make cholera toxin. In the presence of this toxin, chloride ion channels in cells of the small intestine lining are stuck in their open position. As a result, an excess of chloride ions (Cl) flows from these cells into the lumen of the small intestine. Movement of Cl creates a charge gradient, so sodium ions (Na+) also flow into the lumen. Explain why the movement of these ions into the lumen results in the life-threatening diarrhea that characterizes cholera.The amino acid sequence of three peptide fragments are shown below. Peptide 1: QAMGRAGDLKYLGLHSV Peptide 2: ALMALFMVMALVLVSVLFIA Peptide 3: MVEDLLKQIARYLISE (a) Circle all of the charged residues in peptide 1 (assume pH =7.0). Box all of the aromatic residues in peptide 2. Underline all of the nonpolar residues in peptide 3. (b) Determine the net charge of the predominant form of each of the peptides at pH 4.5 and pH 11.5. Assume the ionizable groups have the pKa values listen in Table 2.1 of your text. (c) Which of these peptides would be most likely to be found as an alpha helix in a soluble (cytoplasmic) protein? Which would be most likely to be found as an alpha helix in a transmembrane protein? Which would be least likely to form an alpha helix of any kind?1. A certain polypeptide was treated with trypsin and yielded the following Fragments: Leu-Glu Gly-Tyr-Asn-Arg Gln-Ala-Phe-Val-Lys The same polypeptide was treated with chymotrypsin and yielded the following fragments: Gln-Ala-Phe Asn-Arg-Leu-Glu Val-Lys-Gly-Tyr What is the amino acid sequence of this polypeptide? Instructions Make use of the table below to determine the sequence of the mystery protein.