Batangas State University

College of Nursing and Allied Health Sciences

Pablo Borbon Main I, Rizal Avenue, Batangas City, Batangas, Philippines
Tel No: (043) 300-2202 loc. 120, (043) 300-2273 loc. 1127 Email: batstateu.conahs@gmail.com

LABORATORY EXERCISE FOR WEEK 6:

PROBLEM-SOLVING EXERCISES FOR AMINO ACIDS (PART 2)

Grading Criteria:
• IF with completely correct explanation : 4 pts
• IF explanation is correct but needs further elaboration/clarification – 3 pts
• IF some parts of the explanation are correct but some are erroneous – 2 pts
• IF all explanations are wrong/irrelevant - 1 pt

NOTE: All answers must be handwritten and photographed clearly using CamScanner or
other scanning applications producing high resolution pictures.

Directions: Answer the following as correctly and as comprehensively as possible.

1. Use Fischer projections to show the stereochemistry of D- and L-amino acids. (1 pt for each
correct illustration, total of 20 pts)

2. Explain which amino acids are acidic, which are basic, and which are neutral. Use the isoelectric point
to predict whether a given amino acid will be positively charged, negatively charged, or neutral at a
given pH. Make a table to show these characteristics. Use the format below:

Name of Amino Acid Acidic Basic or Neutral? Positively/Negatively-

(Enumerate the 20 amino (1pt) Charged?
acids) (1pt)
1. Glycine Non
2. Alanine Non
3. Valine Non polar
4. Leucine Non Polar
5. Isoleucine Non Polar
6. Serine Polar, non charge
7. Threonine Polar, non charge
8. Phenylalanine Neutral Non polar
9. Tyrosine Non polar
10. Tryptophan Non Polar
11. Histidine Positive
12. Proline Non polar
13. Hydroxyproline Neutral
14. Cysteine Polar, no charge
15. Methionine Non polar
16. Aspartic acid Nega
Acidic
17. Glutamic Acid Nega
18. Arginine Posi
19. Lysine Basic Posi
20. Hydroxylysine Posi

3. Predict products of the following reactions of amino acids:

(a) Esterification (c) Reaction with ninhydrin
(b) Cylation
 4pts each

4. Discuss and identify the four levels of protein structure:

(a) primary
(b) secondary 4pts each
(c) tertiary
(d) quaternary

 The primary structure is the sequence of amino acids that make up a polypeptide chain.
 Protein secondary structure refers to regular, repeated patterns of folding of the protein
backbone.
 Tertiary structure refers to the overall folding of the entire polypeptide chain into a
specific 3D shape.
 The quaternary structure describes the way in which the different subunits are packed
together to form the overall structure of the protein.

5. Explain how each structure (see letter a to d of item no. 4) of a protein affects its properties and how
denaturation changes the structure. (4pts each)

TOTAL OF 104/104 POINTS

© Wade, Jr. L.G., (2010), Organic Chemistry, 7th Edition, Pearson Education Publishing

Ad Majorem Dei Gloriam!

L - amino acids