Look at the structure shown below and answer the following questions: HN NH но NH Download image. a. The structure shown on the scheme is |(select from: oxytocin, arginine vasopressin )
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- You have a soluble protein that is highly flexible and is only 23 kDa in size. What is the most suitable technique (X-ray crystallography, NMR, cryo-EM) for structure determination of this protein? Explain your reasoning.What could be the implications if there is a misfolding in the protein structure?Illustrate the structure of a peptide with the given sequence below at the given conditions. Serine-Threonine-Glutamic Acid-Lysine-Aspartic Acid-Arginine Form with net charge: -1 Form with net charge: +3 Dominant form at pH 7
- Which of the numbered bonds in this polypeptide fragment are peptide bond(s)? (Select all that apply!)You are working in a bioengineering lab, and you are asked to create a peptide with a helix with length of 3 nm, a beta strand with length of 35 Å, and a linker containing 25 amino acid residues. a. How many amino acid residues are in this peptide? b. What is the mass of the peptide? 2. Why is quinary structure necessary for a full understanding of how drugs work in cells?In the given structure below, 1. What protein was used as the template for modelling the structure of the assigned amino acid sequence? 2. How many alpha-helices and beta-sheets are there?
- Please calculate and plot the charge on a peptide with the sequence of NEYK over the pH range from 1 to 13. Please use the pKa values from the table. You may calculate the charge at 1 pH unit intervals.What if the protein does not have a primary structure, what is its implication? Explain and give example.What is the primary reason the a-helix conformation in polypeptides such a stable form? A. The a-helix structure is stabilized by hydrophobic interactions. B. The a-helix structure is stabilized by intra-helical hydrogen bonds. C. The a-helix structure is stabilized by disulfide bonds. D. The a-helix structure is stabilized by proline residues.
- Consider the following peptide to answer the questions below: A M A K K E S H I F T A I D E What is the total charge of this peptide at pH = 5? What is the N terminal amino acid (full name)? C terminal amino acid? How many fragments would result if this peptide underwent proteolytic cleavage with V-8 protease and what are these fragments (list them)? Would this peptide be a candidate to form an alpha helix? Why or why notDraw the structure of the amino acid(Arginine) at the pH of 8.55Calculate the Rf values for each of the amino acids and enter your data in the table.Based on your calculations, what is the identity of the Unknown amino acid? Rank the amino acids from most hydrophilic to most hydrophobic