Using the letter “R" to indicate amino acid side chain, draw the following: A. The backbone atoms and bonds of a parallel ß-sheet with two B-strands of 5 amino acid each (use slide 23 of Chapter 6 for guidance). B. The backbone atoms and bonds of an antiparallel B-sheet with two B-strands of 5 amino acid each (use slide 23 of Chapter 6 for guidance). C. Draw the hydrogen bonds connecting the two B-strands in each ß-sheet.

Draw the L enantiomer in a Fischer projection for each amino acid; identify the amino acid as neutral, acidic, or basic. Give the three-letter sign [3], and the one-letter symbol [4].arginine a. arginine b. arginine c. a. glutamic acid b. glutamic acid c. glutamic acidtyrosine b. valine c. arginine

1. Label the ALPHA-Carbon, AMINO Group, CARBOXYL Group, and AMINO Side Chain of the following amino acids:- Proline- Glycine- Aspartic acid- Asparagine- Lysine 2. Write the structure of the following polypeptide chainsa.) Asp-Leu-Serb.) Thr-Trpc.) Gln-Ala-Prod.) Ile-Met-Cys-Glu

4. You're working on a structure of a protein and its folding. You think that the interaction between Asp123 and Arg29 is important in determining the structure of the protein. a) What type of amino acid is Asp (acidic, basic, hydrophobic, or polar)? b) What type of amino acid is Arg (acidic, basic, hydrophobic, or polar)? c) What is the strongest interaction that can form between Asp123 and Arg29? You create a mutant Arg29> Lys d) What type of amino acid is Lys (acidic, basic, hydrophobic, or polar)? e) Would you expect this substitution mutation to cause major folding problems? Why or why not? You create mutant Arg29> Glu you discover that this mutant is unable to fold properly, so the protein is nonfunctional. f What type of amino acid is Glu (acidic, basic, hydrophobic, or polar)? g) How does this amino acid substitution cause the protein to fold incorrectly? You find another mutant that also as the same Arg29> Glu mutation. However, this mutant protein įs able to fold normally.…