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- 24. What is the quaternary structure of a protein? Do all proteins have quaternary structure?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?
- 11. Which of the following correctly illustrates a dipeptide and an amino acid in the optimal position to form a tripeptide? (A) R H H-N-C C-N-C Н— N— С OH OH н н H H H. (В) (R® (R R C-N- N Но OH HO OH H. H. H. (C) R H H. Н— N— С C С —С —N — H Н— N— С С—Н H. H. H. H. H (D) R H (R) C-N С—С —N —H Н— С —С HOʻ н н H. H H 0=U11. Below is a folding energy funnel describing folding energy landscape of a protein. The width of the funnel indicates the entropy of the protein, and the height corresponds to the free energy. A) If A is the native fold structure, which state is a molten globule? How does this state differ from A in term of structures. B) Does this protein have multiple folding pathways or just one? C) which state has the lowest free energy? D) According to the width of the funnel, the native state B of the protein has the lowest entropy. If the protein fold A spontaneously to this state, does it violate the 2nd law of thermodynamics? Why or why not? (Hint: in the folding funnel, only the entropy of the protein alone is considered). E) Does the native state also have the lowest enthalpy. What makes the enthalpy decrease as the protein folds? 12. List four methods by which a protein can be denatured and briefly describe how these methods act to disrupt protein structure.2. Calculate the pI of the following primary structure of protein A) Lys- Gly- Ala- Gly B) Lys- Gly-Ala-Glu C) His- Gly- Ala- Glu D) Glu- Gly- Ala -Glu E) Gln-Gly-Ala-Lys
- 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.2) What is glycoside ? In neutral and basic solutions, glycosides do not show mutarotation. However, if the solutions are made acidic, glycosides show mutarotation. Explain why? And write a mutarotation mechanism.Why is the ionic bond between, say, the side chain of lysine and the side chain of glutamic acid stronger in the hydrophobic interior of a protein than in aqueous solvent (water)?
- 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 conformationWhy is the 3-Dimensional structure important for protein function? What factors or agents can denature protein structure? Give examples (more than one factor) Why denaturation affect the function of proteins? Explain the structure - function relationship.Consider beta-sheet comprised of twelve amino acid residues (two strands of six residues each). How many hydrogen bonds should be formed between backbone atoms in this sheet?