Explain why amino acid can increase blood glucose. Write the structure of each of the following peptide at pH7 and identify how many peptide bond in each number. Alanyl-phenylalanine- aspartate- cysteine Threonyl- Isoleucyl-methionyl- leucine Lysyl-alanine -Phenylalanyl-tyrosyl- serine
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- Explain why amino acid can increase blood glucose.
- Write the structure of each of the following peptide at pH7 and identify how many peptide bond in each number.
- Alanyl-phenylalanine- aspartate- cysteine
- Threonyl- Isoleucyl-methionyl- leucine
- Lysyl-alanine -Phenylalanyl-tyrosyl- serine
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- Write the structure of the following peptides: 1. glycyl alanine 2. tyrosyl alanyl glycine 3. phenylalanyl tyrosyl seryl histidine 4. valyl glycyl cystein 5. seryl methionineWrite the chemical structure of peptide containing the following amino acid PRO-SER-GLY-LEUDraw the structure of the following: (in the image provided)Use the amino acids below.F - PhenylalanineI - IsoleucineG - GlycineH - HistidineT - ThreonineE - Glutamic acidR - Arginine
- Write the structure of the following peptides: a) glycyl alanine b) tyrosyl alanyl glycine c) phenylalanyl tyrosyl seryl histidine(a) Draw the structure of the two possible dipeptides that can be formed by combining glycine and asparagine. (b) In each dipeptide, label the N- and C-terminal amino acids. (c) Name each peptide using three-letter symbols.Consider the peptide L-E-T-S-P-R-A-Y Which amino acid(s) is/are basic? A. Y B. P C. R D. L E. T F. S C. A H. E
- Identify the amino acids contained in each of the following tripeptides.What is the net charge at pH 7 on a peptide with the following sequence? Gly-Ala-Lys-Phe-Asp-Met-Val-Pro-Arg-Ala-LeuDraw the peptide ASK(ala-ser-lysine) with proper stereochemistry? what is its pI(isoelectric point)and why the structure is planar? Use the following table to look at pka's of the amino acids and solve this question.
- Write the structure, identify the groups and describe the chemical properties of these amino acids. A. alanine B. Serine C. Leucine D. Phenylalanine E. TryptophanDraw the structural formulas of the following peptides, andshow which bond would be cleaved by chymotrypsin.a. trp-val-glyb. phe-ala-proDetermine the amino acid sequence of a polypeptide from the following data:Complete hydrolysis of the peptide yields Arg, 2 Gly, Ile, 3 Leu, 2 Lys, 2 Met, 2 Phe, Pro, Ser, 2 Tyr, and Val.Treatment with Edman’s reagent releases PTH-Gly.Carboxypeptidase A releases Phe. Treatment with trypsin yields the following four peptides:1. Gly-Leu-Tyr-Phe-Lys 3. Val-Ile-Arg2. Ser-Met-Gly-Leu-Tyr-Lys 4. Met-Leu-Pro-Phe