Enzymes (1)
What is the name of the molecule enzymes bind to, and which part of the enzyme binds to this molecule.
substrate, active
Daily double- Describe what happens to an enzyme when it is exposed to conditions outside their optimum pH or temperature range.
Enzyme will denature, therefore lose function.
Why do lipids have to be packaged into lipoproteins when lipids are in circulation?
Lipids are hydrophobic, and blood is mostly made of water, so lipoproteins are vesicles that shield the lipids from water.
What is the difference between a non-essential and essential amino acid
non-essential amino amino acid your body can produce naturally, essential amino acid you have to acquire from your diet
describe the fluid mosaic model of the cell membrane
Made of lipids and proteins that move around
1. Compare and contrast cofactors and coenzymes
2. What is an apoenzyme what is a holoenzyme
1. Both bind to the enzyme and activate the enzyme (turn the enzyme on)
Cofactors are metallic ions, coenzymes are vitamins
2. Apoenzyme is inactive since a coenzyme or cofactor is not bound to it. Holoenzyme is active since a cofactor or coenzyme is bound to it.
Compare and Contrast competitive and Non-Competitive inhibitors.
Competitive inhibitors mimic the substrate and both have an affinity for the active site. These are reversible by adding more substrate.
Non-competitive inhibitors bind outside the active site, therefore denaturing the enzyme. These are irreversible
2. What type of chemical links two amino acids together?
3. What type of chemical bond holds a triglyceride together?
1. glycosidic
2. peptide
3. ester
Daily double -Explain when a protein folds where the hydrophobic and hydrophilic amino acids are located
Hydrophobic amino acids are located inside the protein away from water, while hydrophillic proteins are located on the outside where they can interact with water
Describe three ways to increase the fluidity of a cell membrane.
decrease both cholesterol and saturated fatty acids, increase unsaturated fatty acids.
1. Describe how the following conditions would increase or decrease the reaction rate of an enzyme.
A. Increase temperature above the optimum temperature
B, Decrease the pH below the optimum pH
C. Add more substrate
D. Add more product
2. Explain what happens during the saturation point in an enzyme reaction
A. Decrease
B. Decrease
C. Increase
D. Increase
2. All of the active sites our occupied with substrate
Compare and Contrast the lock and key with the induced fit theory.
Lock and key is the old model and it's a ridged interaction between substrate and active site. Induced fit theory the active site is flexible to bind the substrate in a perfect orientation.
What are the functions of tri-glycerides
2. What is the main function of phospholipids
3. What are four functions of cholesterol
1. Long-term energy storage, insulation
2. Make up cell membrane
3. Make up cell membrane, make vitamin D, makes bile, makes testosterone, and estrogen
What four properties can the "R" groups have.
1. Polar
2. Non-Polar
3. + charge
4. - Charge
Describe in detail why both phospholipids and integral proteins are amphiphilic.
Have both polar and non-polar part. Phospholipid head is polar, fatty acid tail non-polar. Interior of integral protein non-polar, exterior polar.
What is the purpose of enzymes, and how do they carry out this process
speed up chemical reactions, lower the activation energy
Describe in detail what happens to the reaction rate as you increase the substrate concentration.
Initially as you add more substrate the reaction rate will increase. Eventually all the active sites will be occupied by substrate , therefore the reaction reaches a saturation point and the reaction rate plateaus.
Identify these three structures
1. triglyceride
2. steroid
3. polysaccharide
What are four types of chemical bonds that can hold together the " R " together in the teritary structure of a protein
1. Hydrogen bonds
2. Disulfide Bonds
3. Hydrophobic Interactions
4. Ionic bonds
Explain the differences between phagocytosis, pinocytosis, and receptor- mediated endocytosis.
Phagocytosis transport large solid molecules such as bacteria, polysaccharides, proteins. Pinocytosis transports bulk liquids, receptor-mediated endocytosis transport viruses by specific interaction between receptor on host cell and spike protein on virus.
Describe how feedback inhibition works, and what is the purpose of feedback inhibition.
Feedback inhibition is when the final product inhibits the first enzyme of a pathway. The purpose of feedback inhibition is to conserve energy and resources when enough product is produced.
Would happen only in a closed container as all the ethanol and CO2 that was produced would build up and inhibit the first enzyme of the pathway.
ompare and contrast type i and type 2 diabetes
Type I is an autoimmune disease that results in death of beta cells, therefore decrease insulin production. As a result less glucose delivered into cells and hyperglycemia. Cells use fats as an energy source that will produce ketone bodies that will eventually cause ketoacidiosis.
Type II insulin receptors are resistant to insulin. Since cells are not responding to insulin, beta cells think they need to produce more insulin. Eventually Beta cells are overworked resulting in apoptosis of the beta cells, therefore less insulin prodiced.
Both result in hyperglycemia and ketoacidiosis.
1. Describe the primary structure of a protein
2. What are the two types of secondary structure of a protein and what determines what type of secondary structure the protein, and what do both types of secondary structure have in common.
3. Describe the tertiary structure of a protein and list 4 types of chemical bonds that hold them together
4. Describe the quaternary structure of a protein
. Amino acid sequence
2.
alpha helix or beta sheet
primary structure
both held together by hydrogen bonds between the carboxyl and amino groups
3. Final 3D folding of a protein in which the R groups interact
disulfide bonds, ionic bonds, hydrophobic interactions, hydrogen bonds
4. Proteins that have more than one polypeptide chain.
Compare and contrast simple diffusion and facilitated diffusion.
1. Both high to low, both no energy
2. Simple through phospholipid bilayer, small/non-polar molecules, facilitated through a transport protein large/polar molecules.