Structure of biomolecules and Biorecognition. Amino Acids, Peptides and Proteins. Part 2

Structure of biomolecules and Biorecognition. Amino Acids, Peptides and Proteins.  Antibodies.  Enzymes. Nucleic Acids. Biorecognition: Enzyme/Substrate. Antigen/antibody. Hybridization. Other affinity interactions in nature. Strept(avidin), Protein A and G. Aptamers.  Biomimetic recognition. The importance of water in biorecognition. Biological buffers.

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This lecture will be focused on the structure of proteins. Today we are going to study the folding of proteins into tertiary and quaternary structure and the importance of this folding in the function.


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1. Large, Y shaped protein used by the immune system to identify and neutralize foreign objects such as pathogenic bacteria and viruses
2. Large biomolecule, or macromolecule, consisting of one or more long chains of amino acid residues
3. Protein that acts as biological biocatalyst
4. The first level of protein structure
5. Basic, positively charged amino acid
6. Secondary protein structure
7. Type of beta sheet
8. Protein structure of the virus
9. Loss of structures results in loss of...
10. Protein denaturation agent
11. Amino acid that can form a reversible disulfide bond
12. Secondary protein structure
13. A molecule that contains an equal number of positively and negatively charged functional groups

Self assessment quiz

This test will be open 20/02 at 11:00 am and deactivated at 20/02 23:59.

  • The test has 15 random questions from a pool.
  • This part is done with limited time (30 min).
  • Expected resolution time: 20 minutes.

Note!! After timer finished countdowning, quiz will be submitted automatically

Quiz 1 - Protein structure

Self Assessment Test. This test will help you to revise the structure of the proteins.

15 questions in 1 page and 30 min!

Hint 1. the response can be multiple or, in most of the instances, simple. You will notice by clicking twice if the question admit only one, or more responses.

1 / 15

All hydrophobic amino acids (valine, leucine, isoleucine, etc.) share which of the following properties?

2 / 15

The quaternary  structure of a protein refers to:

3 / 15

Two or more polypeptides attached together and work as one unit

4 / 15

You are given the amino acid sequence Ala-Gly-His-Tyr. This is an example of which level of protein structure?

5 / 15

What is the monomer (building block) of a protein?

6 / 15

The tertiary structure folding in proteins is mainly due to the interactions of....

7 / 15

Amino Acids: Which of the following amino acids can form BOTH hydrogen and ionic bonds?

8 / 15

The pleated sheet is an example of which of the following structural properties of proteins?

9 / 15

Protein denaturing agent(s) (multiple questions)

10 / 15

All proteins have a Quaternary structure.

11 / 15

The unique cyclic structure of which of the following amino acids plays a central role in the formation of alpha helices and beta sheets, due to  it's ability to make sharp turns and commonly being found at the beginning of alpha helices or at the turns in beta sheets?

12 / 15

Which of the following amino acids is NOT charged at physiological pH?

13 / 15

What type of protein organization is shown?

Question Image

14 / 15

In the crusade to create a vaccine for Sars-CoV-2,  a vaccine was created that proved to be successful in preventing COVID onset. The vaccine, which is given by standard injection, contained virus particles inactivated by an organic reagent.  The organic reagent used to inactivate the Sars-CoV-2 virus  in the vaccine significantly alters the viral capsid. For the purposes of this question, let us assume that the capsid proteins are bound together by multiple di-sulfide bonds. Given this information, which of the reagents listed below would be most effective in disrupting the Sars-CoV-2 capsid? 

15 / 15

Hydrogen bonding between separate subunits of DNA polymerase is an example of which of the following?

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