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- 1. The stability of an a-helix is not affected by which of the following? a) Bulkiness b) Occurrence of alanine and glycine residues c) Electrostatic repulsion d) Interaction between R groups spaced three residues apart4. Which of the following polypeptides is capable of forming the most stable alpha helix? a) EEEEEE at pH 7 d) at pH 2 e) PPPPPP at pH 7 b) KKKKKKK at pH 7 EEEEEE at pH 2 5/6. Explain your answer to the previous question. 7. Which of the following is NOT true of a collagen helix or collagen? a) A collagen helix cannot contain prolines. b) A collagen helix has a special amino acid called Hyp c) Collagen is a fibrous protein d) In collagen three helices come together to form a triple helix 8. Which of the following CANNOT make a H-bond. More than one can be circled. a) N-HO=C b) N…H-O-H Ⓒ)C=O....N-C d)C=O....H-O- 9. Which of the following statements describes an apoenzyme? a) the place where a substrate binds b) an apoenzyme is an organic molecule that an enzyme needs to function correctly an apoenzyme is an enzyme that does not have its cofactor and therefore is not functioning it describes a theory on how substrates and enzymes interact.8. NMR measurements have shown that poly-lysine is a random coil at pH 7 but becomes a helix when the pH is raised above 10. If the same type of folding behavior is observed, what should be the pH dependence of poly-glutamate? A) Helix at pH 7 but random coil at pH 10 B) Random coil at pH 3 but helix at pH 7 C) Random coil at pH 7 but helix at pH 10 D) Helix at pH 3 but random coil at pH 7
- 1. Hydrogen bonds can form an alpha helix or beta sheet. The hydrogen atom has a partial positive because of the atom it is covalently bound to. Name the two most common atoms hydrogen bonds within biological systems that give hydrogen a partial positive charge. 2. Are the atoms named in the question above in the backbone of the protein or are they found in R groups? Which R groups? 3. Besides hydrogen, what other atom is involved in the hydrogen bonds in an alpha helix or beta sheet? In other words, hydrogen is interacting with what other atoms when it makes a hydrogen bond? 4. Write out, in order, the full names of the seven amino acids circled in the picture.1. Which best describes the contribution of primary (1’) structure of polypeptides to the native conformation of proteins: a) Structure that results from intrachain interactions of amino acid side chains b) Structure that results from interchain interactions of amino acid side chains c) Structure that results from base pairing d) Structure that results from the linear sequence of amino acids from beginning to end of molecule. 2. What shapes result from secondary structure: a) β- helix & α-sheets b) α-helix and β-sheets c) ɗ-bilayers & β-domains d) µ-folds 3. Which best describes the contribution of tertiary (3’) structure of to the native conformation of polypeptides and proteins: a) Structure that results from intrachain interactions of amino acid side chains b) Structure that results from interchain interactions of amino acid side chains c) Structure that results from base pairing d) Structure that results from the linear sequence of…2. A functional protein that is approximately 110 kDa in size has all its cysteine residues joined with disulfide bonds. It has one cysteine residue per 100 amino acids. When heated at 85°C it lost activity, but when it was allowed to cool, the activity was restored? Please answer the following questions: a) How many disulfide bonds the protein has? Show how you came up with the answer. b) What is the molecular basis for the protein behavior in restoring activity?
- 4. Which best describes the contribution of quaternary (4’) structure of polypeptides to the native conformation of proteins: a) Structure that results from intrachain interactions of amino B) Structure that results from interchain interactions of amino acid side chains c) Structure that results from base pairing d) Structure that results from the linear sequence acid side chains of amino acids from beginning to end of molecule6. A control phospholipid membrane is isolated in which the phospholipid tails all have an 18-C chain length and are comprised of a 50:50 mixture of saturated and unsaturated tails. In addition, about 25% of the lipids are fluorescently labeled on the head groups. a) Draw a single plot of Fluidity vs. Temperature that contains the expected curves for: Control phospholipid (line- -) Control supplemented with 18-C saturated phospholipids (dashed line - Control supplemented with 16-C chain length (dotted line • • • • • • ) b) Draw a single plot of the Fluorescence Intensity vs. Time that contains the expected curves of a Fluorescence Recovery After Photobleaching (FRAP) using the same samples as in (a) above. The FRAP experiment is conducted at the same temperature for each sample (which is the Tm of the of the control phospholipid).8. The following proteins represent a wide range of molecular weights and isoelectric points. 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 pH 8? Explain your answer. d. In what order will these proteins salt out from a pH 7 solution by the dropwise addition of saturated ammonium sulfate? Explain your answer. 83°F 立
- 2. | Calculate the overall charge (pH 7) on the following three polypeptides and answer the questions below. Assume the following pKa values: N-terminal –NH3®, 7.0; all -COOH groups, 4.0; Arg, 12.5; Cys, 8.4; His, 6.0; Lys, 10.0; Tyr, 10.0. (A) Ser-Tyr-Ser-Met-Glu-His-Phe-Arg-Trp-Gly-Lys–Pro–Val–Gly–Lys–Lys–Arg-Arg-Pro-Val-Lys–Val-Tyr-Pro-Asp-Ala -Gly- Glu-Asp-GIn– Ser-Ala-Glu-Ala-Phe-Pro-Leu-Arg-Glu-Phe (B) Ser-Tyr-Ser-Met-Glu-His-Phe-Arg-Trp-Gly-Ala-Pro-Val-Gly-Glu-Glu–Cys-Asp-Pro-Val-Glu–Val–Tyr-Pro-Asp- Ala-Gly-Glu-Asp-Gln-Ser-Ala-Glu-Ala-Phe-Pro-Leu-Glu-Phe-Cys-Ser-Tyr-Ser-Met-Glu–His-Phe-Asp-Trp-Gly- Asp-Pro-Val-Gly-Pro-Asp-Ala-Gly-Asp-Gln-Pro-Val–Gly–Glu-Glu-Cys-Asp-Pro–Val-Glu–Val–Tyr-Pro-Asp-Ala (C) Gly-Ser-Val-Arg-Asp-Pro-Val-Lys-Glu-Val-Tyr-Pro-Asp- Lys–Ala-Gly-Arg-Glu-Ser-Arg-Ala (d) Which of the three peptides would migrate the closest to the anode in isoelectric focusing? (e) Which of the above peptides would elute last from a gel filtration column? (f) Which of the three…2. | Calculate the overall charge (pH 7) on the following three polypeptides and answer the questions below. Assume the following pKa values: N-terminal -NH3®, 7.0; all -COOH groups, 4.0; Arg, 12.5; Cys, 8.4; His, 6.0; Lys, 10.0; Tyr, 10.0. (A) Ser-Tyr-Ser-Met-Glu-His-Phe-Arg-Trp-Gly-Lys-Pro-Val-Gly-Lys-Lys-Arg-Arg-Pro-Val-Lys-Val-Tyr-Pro-Asp-Ala -Gly- Glu-Asp-Gln- Ser-Ala-Glu-Ala-Phe-Pro-Leu-Arg-Glu-Phe (B) Ser-Tyr-Ser-Met-Glu–His-Phe-Arg–Trp–Gly-Ala-Pro-Val-Gly-Glu-Glu-Cys-Asp-Pro-Val-Glu–Val-Tyr-Pro-Asp- Ala-Gly-Glu-Asp-Gln-Ser-Ala-Glu-Ala-Phe-Pro-Leu-Glu-Phe-Cys-Ser-Tyr-Ser-Met-Glu-His-Phe-Asp-Trp-Gly- Asp-Pro-Val-Gly-Pro-Asp-Ala-Gly-Asp-Gln-Pro-Val-Gly-Glu-Glu-Cys-Asp-Pro-Val-Glu-Val-Tyr-Pro-Asp-Ala | (C) Gly-Ser-Val-Arg-Asp-Pro-Val-Lys-Glu–Val-Tyr-Pro-Asp- Lys-Ala-Gly-Arg-Glu-Ser-Arg-Ala (a) Which of the three peptides would elute first from a gel filtration column? (b) Which of the three peptides would migrate the fastest on SDS-PAGE (c) Which of the three peptides could be…2. | Calculate the overall charge (pH 7) on the following three polypeptides and answer the questions below. Assume the following pKa values: N-terminal -NH3®, 7.0; all -COOH groups, 4.0; Arg, 12.5; Cys, 8.4; His, 6.0; Lys, 10.0; Tyr, 10.0. (A) Ser-Tyr-Ser-Met-Glu–His–Phe–Arg–Trp-Gly-Lys-Pro–Val-Gly-Lys-Lys-Arg-Arg-Pro–Val-Lys-Val-Tyr-Pro-Asp-Ala -Gly- Glu--Asp-Gln- Ser-Ala-Glu-Ala-Phe-Pro-Leu-Arg-Glu-Phe (B) Ser-Tyr-Ser-Met-Glu-His-Phe-Arg-Trp-Gly-Ala-Pro-Val-Gly-Glu-Glu-Cys-Asp-Pro-Val-Glu-Val-Tyr-Pro-Asp- Ala-Gly-Glu-Asp-Gln-Ser-Ala-Glu-Ala-Phe-Pro-Leu-Glu-Phe-Cys-Ser-Tyr-Ser-Met-Glu-His-Phe-Asp-Trp-Gly- | Asp-Pro-Val-Gly-Pro-Asp-Ala-Gly-Asp-Gln-Pro-Val-Gly-Glu-Glu-Cys-Asp-Pro-Val-Glu-Val-Tyr-Pro-Asp-Ala (C) Gly-Ser-Val-Arg-Asp-Pro-Val-Lys-Glu–Val-Tyr-Pro-Asp- Lys-Ala-Gly-Arg-Glu-Ser-Arg-Ala 11. - - I C'IL- - 1! (e) Which of the above peptides would elute last from a gel filtration column? (f) Which of the three peptides would migrate the slowest on SDS-PAGE (g) Which of the three…