Quiz in Chemical Biology 3

Name: JAY-AR D. MALANA Date:03-12-2021

Course: BS Biology 2-C

I. Answer the following questions briefly:(10 points each)

1. What two non-standard amino acids are present in Collagen?

4-hydroxyproline and 5-hydroxylysine are the two non-standard

amino acids present in collagen. These amino acids are derivatives of the
amino acids proline and lysine respectively.

2. Where are the carbohydrate units located in collagen?

Carbohydrate units in glycoproteins are attached either to the amide

nitrogen atom in the side chain of asparagine (termed an N-linkage) or to the
oxygen atom in the side chain of serine, threonine, hydroxylysine (termed an
O-linkage). In collagen, since it is O-linked, carbohydrate units are specifically
located or attached to the galactose to hydroxylysine side chains.

3. What is the function of carbohydrate groups present in collagen?

Carbohydrate groups present in collagen is responsible for the high

viscosity and water binding capacity of glycoproteins. It is also responsible in
the folding, conformation, and stabilization of membranes of collagen. Lastly,
it also serve for biological recognition wherein they serve as recognition
determinants in glycoproteins in solution as well as on cell membranes, where
they also exist as glycolipids.

4. What is the role of vitamin C in the biosynthesis of collagen?

It stabilizes the collagen by a process called hydroxylation and is also

responsible for the stimulation of collagen mRNA production by fibroblasts.

5. What is the difference between an antigen and an antibody?

An antigen is a substance foreign to the human body (such as a

bacterium or virus) that invades the human body; an antibody is a biochemical
molecule that counteracts a specific antigen.

6. What is immunoglobulin?

An immunoglobulin, also known as antibodies are Y-shaped

glycoprotein molecules produced by plasma cells and generated against, and
capable of binding specifically to an antigen to lock onto it and neutralize it.
7. Describe the structural features of a typical immune-globulin molecule?

Immunoglobulins have:
 4 polypeptide chains: 2 are identical long heavy chains and the other two
are identical short light chains that have constant and variable amino acid
regions;
 1% to 12% by mass carbohydrate content, and;
 a secondary structure (a Y-shaped conformation) with long and short
chains connected through disulfide linkages.

8. Describe the process by which blood immunoglobulins help protect the

body from invading bacteria and viruses.

When the body senses antigens, the immune system works to

recognize the antigens and get rid of them. B lymphocytes are triggered to
make antibodies (also called immunoglobulins) that lock onto specific
antigens.

Although blood immunoglobulins or antibodies can recognize an

antigen and lock onto it, they can't destroy it without help so they need help
from T cells. These T-cells destroy antigens tagged by antibodies or cells that
are infected or somehow changed. T cells also help signal other cells (like
phagocytes) to do their jobs.

In addition, antibodies can also neutralize toxins, activate a group of

proteins called complement that helps kill bacteria, viruses, or infected cells.

9. Describe the general overall structure of plasma lipoprotein.

Lipoproteins are spherical to discoidal in shape with a core of non-

polar lipids, triacylglycerols and cholesterol esters, and a surface monolayer,
~20Å thick, consisting of apoproteins, phospholipids and non-esterified
cholesterol, that serves to conceal the hydrophobic lipids and present a
hydrophilic face to the aqueous phase.

10. In what chemical form does cholesterol usually exist in the bloodstream?

Lipoprotein

Prepared by:

Helen P. Dangani

(Faculty)