Lesson 2 Molecular Interactions

Question 1

Define “Organic Molecules” and “Biomolecules”

Answer 1

Organic molecules are molecules that contain carbon, biomolecules are organic molecules in living organisms

Question 2

What are 4 main biomolecule groups

Answer 2

Carbohydrates (Sugars)
Lipids (Fats/Oils)
Proteins (Polymers of amino acids)
Nucleotides (DNA, RNA, ATP)

Question 3

Can biomolecules be made up of more than one molecule?

Answer 3

Yes. Biomolecules are not always one kind of molecule
Examples of this are Conjugated proteins (Proteins + Biomolecule)
Glycosylated Molecules (Molecules + Carbs)
Polymers (Repeating chain of biomolecules)

Question 4

Define “Covalent Bonds”

Answer 4

Covalent bonds are when two molecules are bonded through the sharing of electrons

Question 5

Name some reasons on how Non-Polar and Polar molecules differentiate from each other?

Answer 5

Polar —> have a net dipole and uneven distribution of molecules
Non-Polar —> Have no net dipole and have even distributions of molecules

Question 6

Define “Ionic Bonds”

Answer 6

Ionic bonds can be defined as the electrostatic attracts between ions

Question 7

What is the main difference between polypeptides and proteins

Answer 7

Polypeptides are made from 10-100 amino acids
Proteins are made of greater than 100 amino acids

Question 8

Differentiate between hydrophilic and hydrophobic substances

Answer 8

Hydrophilic —> Soluble in water (Ions, Polar molecules etc)

Hydrophobic —> Not soluble in water (Non-polar molecules)

Question 9

Define how “Hydrophilic interactions” Work

Answer 9

Hydrophilic interactions occur between water and ions or, other polar molecules. Ions + Polar molecules dissolve in water and create biological solutions

Question 10

What important role do “Nucleotides” play on the body?

Answer 10

They help in energy and information transfer. (Included single nucleotides such as ATP, ADP and AMP)

Question 11

Define phosphorylation and Deposphorylation in simple terms

Answer 11

It is the addition or removal of a phosphate group

Question 12

How does the line structure of Amino Acids look like?

Answer 12

An Amino group (Nitrogen) with one carbon, then a carboxylic acid and a functional group

Question 13

How do the Primary structure of polypeptides look?

Answer 13

They are a chain/sequence of amino acids

Question 14

How does an amino acids secondary structure affect its shape?

Answer 14

It may turn cylindrical or sheeted through the covalent bond angles
Ex: Alpha-Helix
Beta Pleated sheets

Question 15

How do Tertiary structures affect the shape of proteins?

Answer 15

It allows the protein to turn into a 3-dimensional shape
Ex: Fibrous Proteins (Collagen)
And
Globular Proteins (Myoglobin)

Question 16

How does a quaternary structure form?

Answer 16

They form from the combination of multiple subunits with no covalent bonds.
Ex: Hemoglobin is made from 4 globular protein subunits

Question 17

True Or False

The Shape of molecules are closely related to their function

Answer 17

True

Question 18

Define the words “Specificity”, “Affinity”, “Competition” and “Saturation” in relation to proteins

Answer 18

Specificity: The ability of a protein to bind to a certain ligand or a group of closely related ligands
Affinity: The desire/strength for the protein and ligand to bond together
Competition: Ability for ligand to bind to its site while competing with other compounds
Saturation: The amount of points of binding that are available on all proteins

Question 19

True Or False
Proteins affinity for certain ligands can change

Answer 19

True

Question 20

What is the definition of activation in a protein?

Answer 20

Activation is the changing of binding sites in a protein this can be done through Cofactors (Non-protein chemicals that share the binding site) Or allosteric activators (Modulate the protein from any location)

Question 21

What do “Chemical Modulators” do?

Answer 21

They bind reversible or irreversibly to proteins and alter their binding affinity

Question 22

What do antagonists or inhibitors do to proteins?

Answer 22

They are chemical modulators that bind to a protein and decrease its activity

Question 23

Do physical factors have large effects on protein structure and function?

Answer 23

Yes, things such as PH and temperature can modulate protein activity

Question 24

Define the term “Denatured” referring to proteins?

Answer 24

Denaturing proteins is when the shape of a protein gets deformed due to imbalances in the body. (Heat, Ph changes, Chemical denaturing, ETC)