Draw an a amino acid with an isopropyl (-CH(CH3)2) side chain.

Draw the structures of the amino acids formed at physiological pH when the tripeptide below is hydrolyzed. Н Н 0 Н |+ 1 || | H-N-с-с-N-с Н H C CH Н ОН н с Н Н || | | C-N-C-C-0 CH, HC CH Нc CH c=0 с NH₂ ОН

please solve question 1

A peptide has the sequence Ala-Phe-Glu-Lys-Asp-Pro-Asp. What charge will it carry at physiological pH? Show your calculation.

Draw the 3 amino acids formed when this tripeptide is hydrolysed in a boiling solution containing a strong acid.   Circle the R-groups on your answers for question i. and indicate if these R-groups are polar, nonpolar or charged.

Draw a representative amino acid, labelling the side group as R and identifying the amino and carboxylic acid groups.

What does the "alpha" indicate in "α-amino acid"?   That the -COOH group is below the plane of the ring. That the amino group is the first group in the compound. That the alpha-carbon has a -NH2 attached. The the amino acid is the dominant form.

(a) Which amino acid is present in higher amounts than glycine?(b) How many more molecules of that amino acid are presentthan the number of molecules in 1.0 mole of glycine?

True or False

1. Which of the following statements is false? Many peptides come together to form polypeptides. They can form flat networks Proteins contain thousands of peptides cessibility: Good to go These can form an infinite number of configurations. O W (hp