Question 16 Two peptides have almost the exact same primary structure, except that one has about 10 fewer amino acids at the amino-terminus (N-terminus) of the protein. What is a possible explanation for the protein that is missing those 10 amino acids? O A. An alternative Poly-A tail addition site O B. Leaky scanning occurred O.Differential glycosylation of the protein O D. Inefficient folding by chaperone proteins O E. All of the above are correct answers
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- D Question 9 I am an alanine residue present in a peptide with defined secondary structure. I have and dihedral angles of 45° and -45°, respectively. What structure best defines my environment? O B-sheet O B-turn Right handed a-helix O Left handed a-helix O These angles do not correspond to a well-defined secondary structurePage 1 > of 3 ZOOM B. Propose une Toie onsuinin Teguiaung Dioou giucose concentrauon. Question 2: Label the protein structure level on lines 1,2,3, and 4 and label/describe the structure to which each box corresponds. Describe the characteristics of each structural level in the boxes below. MacBook Air DII 80 888 F10 F7 FB F5 F4 F3 * & # $ 7 8 3 4 E R T Y K F M C V .. .. この * 00 BShown below is a portion of primary sequence of a very large protein. -Gly-Pro-Arg-Gly-Pro-Hyp-Gly-Ser-Ala-Gly-Ser-Hyp-Gly-Lys-Asp--- Which of the following structures is most likely formed from this protein sequence? D A. A О В. В OC.C O D. D OE. E B.
- 4. A polypeptide comprised of 17 amino acid res- idues with the sequence on the right is ob-served by spectroscopic methods to undergo transitions from an a-helix conformation to a B-sheet as a function of pH and concentration. The acetyl and carboxamide groups are attached covalently to deri- vatize the N- and C-terminal residues, respectively, to avoid charge effects of the end groups. CH3CO-ΤAΤΚΑE LLAKYEATΗK-CONH2 (a) ( amino acid residues. Write the sequence of this polypeptide with corresponding 3-letter abbreviations for the (b) At pH < 4 the polypeptide forms an a-helix. (i) ( the helix? and (ii) (: · with respect to the positive and negative ends of the macrodipole? ) What is the direction of the macrodipole of | Are the charges on the N- and C-terminal residues stabilizing or de-stabilizing (c) (* stabilize the helical conformation. What are the most likely protonation states of the side-chains that provide a-helix stabilizing interactions? Use the helical wheel (at the back…4. A polypeptide comprised of 17 amino acid res- idues with the sequence on the right is ob-served by spectroscopic methods to undergo transitions from an a-helix conformation to a B-sheet as a function of pH and concentration. The acetyl and carboxamide groups are attached covalently to deri- vatize the N- and C-terminal residues, respectively, to avoid charge effects of the end groups. CH3CO-ETATKAELLAKYEATHK-CONH2 (а) amino acid residues. Write the sequence of this polypeptide with corresponding 3-letter abbreviations for the (b) At pH < 4 the polypeptide forms an a-helix. (i) the helix? and (ii) with respect to the positive and negative ends of the macrodipole? What is the direction of the macrodipole of Are the charges on the N- and C-terminal residues stabilizing or de-stabilizingThe first and major effect in denaturation of proteins is that: a. peptide bonds break. b. helices unwind. c. sheet structures unfold. d. tertiary structure is changed. e. quaternary structures disassemble.
- In the given structure below, 1. What protein was used as the template for modelling the structure of the assigned amino acid sequence? 2. How many alpha-helices and beta-sheets are there?Show below is a polypeptide comprised of 3 α-helices and 5 β-sheets joined by randomcoil. Characterizetheforces that stabilize the tertiarystructure and draw the interacting side chains ofd) Cys Cys7. A peptide has the sequence Cys-His-Glu-Met-lle-Ser-Thr a. Write out the single letter sequence of this peptide. b. What is the overall charge of the peptide? Is it acidic? Basic? c. Draw the chemical structure of the peptide at pH 7.0 and show any charged groups d. What is the classification of each amino acid in this peptide regarding polarity and charge? 8. The following proteins represent a wide range of molecular weights and isoelectricpoints. Mr is the molecular weight of a single protein chain. • Protein 1: Mr 68,544; pl 6.11 (monomer) • Protein 2: Mr 29,041; pl 5.32 (dimer) Protein 3: Mr 15,805; pl 5.7 (dimer) • Protein 4: Mr 12,165; pl 4.74 a. Which protein is the most acidic? Explain your answer. b. Which protein will migrate the slowest in an SDS-PAGE? Explain your answer. c. In what order will these proteins elute from a cation exchanger at phH 8? Explain your answer. d. In what order will these proteins salt out from a pH 7 solution by the dropwise addition of saturated…
- A protein, X, showed only one peptide band in native PAGE at pH 5 7 and 8.5. When the protein was run in SDS-PAGE, the electrophoregram showed 2 bands of MW equal to approximately 2X the size of the untreated protein. What interactions are involved between the monomeric polypeptide components of protein X? O A. H-bonding between cys and his B. Electrostatic interaction between lys and glu O C. Disulfide bonds between cys residues D. Covalent bond between amino acid components of the monomers E. Non-covalent interactions among the amino acids at the interface of the monomersA protein has been sequenced after cleavage of disulfide bonds. The protein is known to contain 3 Cys residues, located as shown below. Only one of the Cys has a free –SH group and the other two are involved in an -S-s- bond.18 The image below shows the different interactions responsible for the spontaneous folding of a protein molecule. Identify which interactions are involved for each labelled region 0-H H CH,OH CH, NH, 0 B O-H--OO CH, CH₂ A B D C A यह मह CH CH₂COOH C H CH, CH, CH, CH H--O=C D T (CHJANH, - interactions ion-dipole interaction Hydrogen bonding Hydrophobic interactions Disulfide bonds lon-ion interaction 18