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- Describe the four levels of protein structure. How do a proteins side groups influence its interactions with other substances? What happens when a protein is denatured?1)Explain 3 benefits of proteins forming higher oligomeric states. 2) Why are peptide bonds planar?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?
- 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. State the four types of attractive interactions that give rise to tertiary protein structure. 3. Can more than one type of secondary structure be present in the same protein molecule? Explain your answer.1. Proteins perform critical functions in all of our cells. Without proteins, life wouldn’t exist. Think of some specific proteins and describe what function they perform. 2. Explain the difference between secondary and tertiary protein structures. 3. How many water molecules are produced when a dipeptide is synthesized?
- 1. How are organic molecules related to all living things?Explain. 2. Draw an Illustration showing the functions of protein in the body.1. Explain how each primary structure of a protein affects its properties and how denaturation changes the structure. 2. Explain how each secondary structure of a protein affects its properties and how denaturation changes the structure.4. Which level of protein structure do proteins need to function (there may be more than one correct answer)? Explain why?
- 1.Describe in detail how to determine the primary structure of protein. 2.You have been given a mixture of lysine, histidine and cysteine.The isoelectric point of the amino acids are as follows; histidine 7.64 lysine:9.74 cysteine:5.02 Show how you will separate the mixture into the pure forms. State and describe any instrument that you will use to separate the components in the mixture.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.4. Each diagram in Figure 2 below shows one level of organization of a protein. Identify each level and describe it. CA ITA (a) (b) 0 hydrogen co CH₂ bond H-0 (c) -0, 0 lonic bond C-OH H₂C H₂C CH-CH₂ amino acids -hydrophobic interactions disulfide bridge Figure 2 5. Hemoglobin is made up of four polypeptides, but also require a beme group
