Lesson 2 Molecular Interactions Flashcards
Define “Organic Molecules” and “Biomolecules”
Organic molecules are molecules that contain carbon, biomolecules are organic molecules in living organisms
What are 4 main biomolecule groups
Carbohydrates (Sugars)
Lipids (Fats/Oils)
Proteins (Polymers of amino acids)
Nucleotides (DNA, RNA, ATP)
Can biomolecules be made up of more than one molecule?
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)
Define “Covalent Bonds”
Covalent bonds are when two molecules are bonded through the sharing of electrons
Name some reasons on how Non-Polar and Polar molecules differentiate from each other?
Polar —> have a net dipole and uneven distribution of molecules
Non-Polar —> Have no net dipole and have even distributions of molecules
Define “Ionic Bonds”
Ionic bonds can be defined as the electrostatic attracts between ions
What is the main difference between polypeptides and proteins
Polypeptides are made from 10-100 amino acids
Proteins are made of greater than 100 amino acids
Differentiate between hydrophilic and hydrophobic substances
Hydrophilic —> Soluble in water (Ions, Polar molecules etc)
Hydrophobic —> Not soluble in water (Non-polar molecules)
Define how “Hydrophilic interactions” Work
Hydrophilic interactions occur between water and ions or, other polar molecules. Ions + Polar molecules dissolve in water and create biological solutions
What important role do “Nucleotides” play on the body?
They help in energy and information transfer. (Included single nucleotides such as ATP, ADP and AMP)
Define phosphorylation and Deposphorylation in simple terms
It is the addition or removal of a phosphate group
How does the line structure of Amino Acids look like?
An Amino group (Nitrogen) with one carbon, then a carboxylic acid and a functional group
How do the Primary structure of polypeptides look?
They are a chain/sequence of amino acids
How does an amino acids secondary structure affect its shape?
It may turn cylindrical or sheeted through the covalent bond angles
Ex: Alpha-Helix
Beta Pleated sheets
How do Tertiary structures affect the shape of proteins?
It allows the protein to turn into a 3-dimensional shape
Ex: Fibrous Proteins (Collagen)
And
Globular Proteins (Myoglobin)
How does a quaternary structure form?
They form from the combination of multiple subunits with no covalent bonds.
Ex: Hemoglobin is made from 4 globular protein subunits
True Or False
The Shape of molecules are closely related to their function
True
Define the words “Specificity”, “Affinity”, “Competition” and “Saturation” in relation to proteins
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
True Or False
Proteins affinity for certain ligands can change
True
What is the definition of activation in a protein?
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)
What do “Chemical Modulators” do?
They bind reversible or irreversibly to proteins and alter their binding affinity
What do antagonists or inhibitors do to proteins?
They are chemical modulators that bind to a protein and decrease its activity
Do physical factors have large effects on protein structure and function?
Yes, things such as PH and temperature can modulate protein activity
Define the term “Denatured” referring to proteins?
Denaturing proteins is when the shape of a protein gets deformed due to imbalances in the body. (Heat, Ph changes, Chemical denaturing, ETC)
