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.
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- 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.1)Explain 3 benefits of proteins forming higher oligomeric states. 2) Why are peptide bonds planar?7/ Hemoglobin is an example of a protein with A. Primary structure only. B. two protein chains held together. C. a quaternary structure. D. primarily a B-pleated sheet structure.
- 3. Why do we need to study the four levels of protein structure? Cite its practical use to our day-to-day life.6.All of the following types of interactions cooperate in stabilizing the tertiary structures of globular proteins except____. a.Disulphide bond b.Hydrogen bond c.Ionic interactions d.Peptide bond1. Describe how each of the following relates to protein configuration: primary structure - secondary structure - tertiary structure - quaternary structure -
- 1. Why do proteins become polycations at extremely low pH and become polyanions at very high pH? 2. Explain why hydrogen bonding is important to protein structure.Compare (4 differences & 4 similarities) between the secondary structure and quaternary structure of proteins1.Describe in detail how to detect the primary structure of protein. 2.Given a mixture of lysine,histidine and cysteine.The isoelectronic 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.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) Describe the importance of the amino acids in the structure such as the alpha helix in the secondary structure; the beta-sheet and the alpha helix in the final tertiary structure. 2) A photo of a 3D tertiary structure model of your protein using paper.7. Native conformation of proteins may result from: a) hydrophobic interactions b) H-bonds c) ionic bonds d) covalent bonds e) all a-d may contribute to native conformation