4.1. From this structure, what is the predominant secondary structure of the protein? 4.2. Based on what you can observe from the protein, what is its highest level of organizational structure? 4.3. If applicable, how many subunits does this protein have and are they identical?
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- 5 (a) Describe in detail how you will determine the primary structure of protein. 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 Cystenie 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.Discuss and identify the four levels of protein structure (primary, secondary, tertiary,and quaternary). Explain how the structure of a protein affects its properties and howdenaturation changes the structure.In regards to the protein structure, explain what is meant by “tertiary structure.” Whatare the main forces that stabilize tertiary structures in proteins? Provide examples.
- In a subunit of a protein, arginine and aspartic acid have an ionic interaction between their side chains. Part a) If arginine is changed to glutamic acid, would the ionic interaction's stability increase, decrease, or not change and what effect would it have on the protein structure? Explain why. Part b) If arginine is changed to lysine, would the ionic interaction's stability increase, decrease, or not change and what effect would it have on the protein structure? Explain why. Part c) If arginine is changed to isoleucine, would the ionic interaction's stability increase, decrease, or not change and what effect would it have on the protein structure? Explain why.Explain what is meant by “The Central Dogma”? In your explanation, describe the structure and function of the macromolecules that are important in this process. Describe at least 4 deviations to the Central Dogma.Draw Ramachandran plot for: a) regular secondary structure with Φ = 60-65 and Ψ = 60-80 b) regular secondary structure with Φ = -170 and Ψ = 170 c) intrinsically disordered proteins d) explain why these Ramachsndran plots will be different, and what secondary structures are described in A and in B
- 1.Here is an oligomeric protein, which has two binding sites:1)Write the formulas of side chains of amino acids which are located in binding sites and suggest two ligands,which can be bound with this protein. 2) Name the types of bonds which will be formed between the ligands and amino acids of binding sites.3)Give the definition of quaternary structure. What do you know about the properties of proteins with the quaternary structure?Based on this table: 1) What is the difference between subunit mass and native mass? 2) How do you tell what the likely quarternary structure of the protein is? (heterotrimer, homotrimer, etc.)At what level of protein structure (primary, secondary, tertiary or quarternary) does Hydrogen bonding is relevant ? Consider if there is no Hydrogen bonding that exists, and only van der Waals exists in this protein structure, what do you expect to happen in its property? Explain with examples.
- The first stage protein is a water soluble protein that has a tertiary structure. Which type of amino acids would you expect to find (i) on the proteins surface and (ii) in the proteins core, explain and justify your answer while giving examplesOur growing understanding of how proteins fold allows researchers to make predictions about protein structure based on primary amino acid sequence data. Consider the following amino acid sequence.(a) Where might bends or β turns occur?(b) Where might intrachain disulfide cross-linkages be formed?(c) Assuming that this sequence is part of a larger globular protein, indicate the probable location (external surface or interior of the protein) of the following amino acid residues: Asp, Ile, Thr, Ala, Gln, Lys. Explain your reasoning.Most proteins denature at high temperatures. A. Are peptide bonds typically broken at high temperatures, yes or no? _________________ B. Does denaturation disrupt the primary structure of a protein, yes or no? __________________ C. Why do proteins denature at high temperatures? D. Is it likely that a denatured protein is able to perform its physiological function, yes or no? Why or why not? Thoughtfully defend your answer.