Macromolecules
What differentiates saturated and unsaturated fatty acids?
* Unsaturated = contains at least one double bond in the hydrocarbon chain.
* Saturated = singles bonds only.
Lecture 2, slide 20
Define an enzyme and explain how the catalyze chemical reactions.
Proteins that facilitate/speed up chemical reactions.
(They lower the activation energy necessary for the reaction to occur).
Lecture 3, slide 29.
Define metabolism.
All chemical reactions that occur in the body.
Lecture 3, slide 40
What are the 3 main components of cells?
Plasma Membrane
Nucleus
Cytoplasm
Lecture 4, slides 6-7
What are the functions of proteins in the body?
Several!
Structure, movement, enzymes, receptors, carriers, signaling molecules, antibodies, etc.
Lecture 3, slide 10
What are the monomers of each class of macromolecules?
* Carbohydrates: Monosaccharides > Glucose, Fructose, Galactose.
* Proteins: Amino Acids
* Nucleic Acids: Nucleotides
* Lipids: Fatty Acids**
** No true monomer
Lecture 2, slides 33 and 42.
Lecture 3, slides 4 and 12.
What R functional group would be present in the active site of a polar substrate? And a negatively charged substrate?
Polar - Polar
Non-polar - Non-polar
Negative - Positive
Lecture 3, slide 7
Differentiate Catabolism and Anabolism. Which release energy?
* Catabolism = breakdown of larger to form simpler molecules > Release energy
* Anabolism = building larger from simpler molecules > Require energy
Lecture 3, slide 40
What are the three types of muscle tissue?
* Skeletal muscle (found around bones, voluntary movement)
* Smooth muscle (found around visceral organs, involuntary movement)
* Cardiac muscle (found on heart walls, involuntary movement)
Lecture 4, slide 4
Define denaturation.
Protein unfolding (loss of function) caused by non-optimal pH, temperature, and [salt].
Lecture 3, slide 8
What are the monosaccharides that comprise maltose, sucrose, lactose, starch, cellulose and glycogen?
Maltose: G - G
Sucrose: G - F
Lactose: G - Ga
Starch, Cellulose, Glycogen: Glucose ONLY.
Lecture 2, slides 33-37
What are the properties of an enzyme? (3)
* They are specific to their substrate
* Reusable (unchanged at the end of reaction)
* Does not change the nature of the reaction (simply speeds it up)
Lecture 3, slide 31
What's a branched metabolic pathway?
One initial substrate can lead to multiple final products.
Lecture 3, slide 41
Which two types of cytoskeleton help with intracellular transport?
Microtubules = Serve as a track for Dynein and Kinesin.
Microfilaments = Serves as a track to Myosin.
Kinesin, Dynein and Myosin are motor proteins.
Lecture 4, slide 13
What level of protein structure is disrupted by denaturation?
Tertiary structure: Non-optimal conditions disrupt intermolecular interactions among R groups.
Lecture 3, slide 8
Differentiate the term Ketosis and Ketoacidosis.
* Ketosis = Production of ketone bodies by the liver when the body has insufficient glucose (e.g.: low carb diet).
Remember: Glucose is the primary fuel source of the body. When glucose source and storage are too low, fatty acids become an alternative energy source.
* Ketoacidosis = Ketone bodies are ACIDIC molecules. Excess amounts can lower blood pH (e.g.: "keto fever").
Lecture 2, slide 43.
What are the factors that affect enzyme activity?
* Temperature and pH (Remember: enzymes are protein and thus can suffer denaturation!)
* Law of mass action (The side of reaction of lower concentration will be favored)
* [Substrate]
* Cofactors and Coenzymes (molecules that attach to an enzyme to make it active).
Lecture 3, slides 34-37
Differentiate Dehydration and Hydrolysis reactions.
* Hydrolysis = Break down of molecules
* Dehydration = Build molecules (formation of bonds)
Lecture 2, slides 35-36
Differentiate mitosis and meiosis. In which type of cell does each occur?
* Mitosis = produces 2 genetically identical cells, and occurs in somatic cells (all cells other than gametes)
* Meiosis = produces 4 genetically distinct daughter cells, and occurs in gamete cells.
Lecture 4, slide 27
Which categories of R groups interact with each other in the tertiary structure of protein folding?
Non-polar - Non-polar
Polar - Polar
Positive - Negative
Lecture 3, slide 7
What are the general functions of each class of macromolecules?
* Carbohydrates: Source of energy, energy storage, fiber, a component of the plasma membrane (ex: glycoproteins).
* Lipids: Energy storage (Triglycerides), a component of the plasma membrane (phospholipids), hormones (steroids), cushioning, and insulation.
* Proteins: Several! Structure, movement, enzymes, receptors, carriers, signaling molecules, etc.
* Nucleic Acids: Forms DNA, RNA, and essential molecules such as ATP.
Lecture 2, slides 32 and 39
Lecture 3, slides 10, 13, 18
How can pathologists detect disease and cellular damage based on the presence of certain enzymes in a person's blood?
Certain enzymes should be found only within cells. If found in the blood, it indicates that the cell suffered lysis and its content leaked into the blood.
e.g.: LDH in blood indicates heart attack.
Lecture 3, slide 32
What is end-product inhibition?
A type of negative feedback to control metabolic pathways: the excess presence of a certain product can inhibit the enzyme that allows for its production.
Lecture 3, slide 43
How do cells specialize in function?
They specialize in function according to the concentration and size of their organelles:
Examples:
Muscle cells: Contain a lot of Ribosomes, so they can produce a high amount of proteins.
Liver cells: Have a well-developed Smooth Endoplasmic Reticulum to detoxify toxins.
Lecture 4, slide 23
Name and explain the four stages of protein structure.
Primary: Sequence of amino acids.
Secondary: Alpha helix and Beta pleated sheets (held by Hydrogen bonds).
Tertiary: Intermolecular interactions among R groups (e.g.: ionic bonding and Hydrogen bonds).
Quaternary: Combination of more than one tertiary structure.
Lecture 3, slide 9