a) Canavanine is an amino acid that is produced by some legume plants. It is not used in proteins but serves as a nitrogen storage molecule in seeds, and is being investigated as a possible anti-cancer and anti-viral drug. Canavanine's amino and carboxyl groups are the same as those in any other amino acid (pKa for the amino group is 8.0 and pKa for the carboxyl group is 3.1), and its side group has a single ionizable group with a pKa of 7.0. Describe or explain what that statement (the previous sentence) tells you about the protonation state of each of the 3 ionizable groups on this amino acid if it is dissolved in pure distilled water at pH 7.0.

For the amino acid alanine, the major species in solution at pH 7 is the zwitterionic form, which has a negatively charged carboxylic acid group and a positively charged amino group. There is a less common neutral form in which neither group is charged. The carboxylic acid group of alanine has a p?a of 3 The amino group of alanine has a p?a of 8 Estimate the ratio of the concentration of the neutral amino acid species to the zwitterionic species at pH 7.   __?__x10^?

Explain why casein precipitates when vinegar is added. Why was milk or raw egg once used as an antidote in cases of heavy metal poisoning? Based on your isolated yield of casein, how many grams of the protein are in one 200 g glass of milk? Which of the solutions contained amide bonds? Which test tells you this? Which of the solutions contained compounds with primary amino groups? Which test tells you this? Describe two examples of protein folding patterns and identify what level of protein structure they belong to. What other reagents might you use besides ferric chloride to test affinity for metal ions?

How is phenyl isothiocyanate useful in determining protein structure?

X The fundamental difference given in the 10 amino acids found in human proteins is given by the R group: True false

All amino acids have two ionizable functional groups: an α‑amino group (average pKa of 9.4) and an α‑carboxylic acid group (average pKa of 2.2). Aspartic acid has an ionizable side chain (R group) with a pKa of about 3.8. One of the possible ionization states of aspartic acid is shown in the image. At what pH would the structure be the predominant ionization state? Consider the ionization state of all three of the functional groups.

Name the following amino acids using their common name

Glycine is a diprotic acid, which can potentially undergo two dissociation reactions, one for the a-amino group (-NH3), and the other for the carboxyl (-COOH) group. Therefore, it has two pKą values. The carboxyl group has a pK₁ of 2.34 and the a-amino group has a pK₂ of 9.60. Glycine can exist in fully deprotonated (NH₂-CH₂-COO-), fully protonated (NH3-CH₂-COOH), or zwitterionic form (NH3-CH₂-COO-). Match the pH values with the corresponding form of glycine that would be present in the highest concentration in a solution of th pH. fully deprotonated form NH,−CH,−COO- pH 11.9 pH 6.0 pH 8.0 fully protonated form NH3-CH₂-COOH pH 1.0 Answer Bank pH 7.0 zwitterionic form NH3-CH₂-COO-