Concept explainers
Interpretation:
The fragments obtained from the cleavage of the given peptide chain by trypsin has to be predicted.
Concept introduction:
Amino acids are linked each other by peptide bonds is called protein (one or more peptide bonds). Peptide bonds are amide bonds, in which carbonyl group of one amino acid bonded to amino group of other amino acid. The chain of the protein is drawn in such a way that left end is occupied by free amino group (say N-terminal) and right side of the chain is occupied by carbonyl group (say C-terminal).
Endopeptidases cleave peptide bonds that are not at the end.
Trypsin is an endopeptidase, which cleave the C-side peptide bond of positively charged side chains such as arginine, histidine and lysine.
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Check out a sample textbook solutionChapter 19 Solutions
Fundamentals of General, Organic, and Biological Chemistry (8th Edition)
- After a polypeptide chain has been synthesized, certain amino acids in the peptide may become modified. For each modified amino acid, identify the standard amino acid from which it is derived. Enter the unabbreviated name of the standard amino acid. OH I *NH,CH,–C–CH,CH,—CH–COO H C *NH₂ standard amino acid: Identify the modification that yields the first amino acid depicted. addition of a hydroxyl group addition of an amino group modification of the existing amino group modification of the existing hydroxyl group elongation of the side chain by the addition of a -CH₂- grouparrow_forwardConsider the following peptide: Lys-Tyr-Glu-His-Arg-Ala-Asp-Arg-Glu-Tyr-Lys a) What is the net charge of this peptide at pH=1? Show your work. b) What is the net charge of this peptide at pH=14? Show your work.arrow_forwardConsider the following two peptides: I. N-Pro-Pro - Glu - Glu - Tyr - His - Cys - Ala - Glu - Gln - Lys - Leu - Ser - Ser - Phe-Leu- Thr - C II. N-Pro-Pro - Lys - Arg - Gly - Tyr - His - Gly - Glu - Asp - Glu - Asp - Glu - Ser - Gly-Phe- Tyr-C Give three reasons why_peptide I is more likely to form an alpha helix in aqueous solution at pH 7.0. Your reasons may include why_peptide Il is less likely to form an alpha helixarrow_forward
- Consider the peptide Asp-Lys-Phe-Glu-Asn-Tyr-Gln-Val-Cys. In a single beaker, you treat this peptide with 2 proteases. One protease cleaves at the N-terminus of aromatic R groups and the other cleaves at the C-terminus of polar, non-ionizable R groups. Following the enzymatic digestion, you want to separate your peptide fragments so that you can identify them. You choose to separate the fragments using an anion exchange column. Beginning at pH=6 you apply your peptide fragments to the column and you gradually decrease the pH of the column stopping the separation when the pH of the column equals 4. Omitting chemical structures, write the amino acid sequence of the peptide fragments that are produced from this digest. Write the order that these fragments will elute from the column (if at all). (Relevant pKa values are: 2.1, 3.8, 4.3, 8.3, 9.6, 10.1, and 10.5)arrow_forwardc=0 OH CH2 H CH2 H CH, H. H-Nt CH' CH N. CH CH CH' H CH CH3 H CH H CH2 CH, CH, CH2 CH2 CH3 CH2 CH2 * NH3arrow_forwardAmino 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?arrow_forward
- Translate the following amino acid sequence into one-letter code: Glu-Leu-Val-Ile-Ser-IleSer-Leu-IleVal-Ile-Asn-Gly-Ile-Asn-Leu-Ala-SerValGlu-Gly-Ala-Serarrow_forwardWhat products are formed when each peptide is treated with trypsin? Be sure to answer all parts. [1] Phe-Leu-Phe-Asn-Lys-Ser [2] Phe-Ser-Thr-Arg-His-Trp [3] Met-Met-Lys-Val-Asp-His-Thr-Thr-Tyr-Ala-Thr-Gluarrow_forwardDraw the peptide formed between asparagine and histidine. H,N- -CH-C-OH H,N-CH-ċ-OH ČH2 ČH, N° NH2 -NH +arrow_forward
- The sequence of a peptide is given below. Ala-gly-val-leu-trp-lys-ser-phe-arg-proWhich peptide bond(s) are cleaved by chymotrypsin(arrow_forwardHow is the peptide shown named (give each 3-letter name for the amino acids present)? Whichamino acid is at the N-terminal? Which amino acid is at the C-terminal?arrow_forwardConsider the following two peptides: I. Ile-Trp-Ala-Met and II. Glu-His-Cys-Thr Which peptide would be more soluble in water? Answer I or II.arrow_forward
- Human Heredity: Principles and Issues (MindTap Co...BiologyISBN:9781305251052Author:Michael CummingsPublisher:Cengage Learning