BioChem C785 - WGU - Module 2 - all questions graded A

BioChem C785 - WGU - Module 2 - all questions graded A Deedra's dad has Alzheimer's Disease (AD) which is caused by a change in protein structure ✔✔True Alzheimer's disease is caused by aggregation of the Amyloid bet ...

BioChem C785 - WGU - Module 2 - all questions graded A Deedra's dad has Alzheimer's Disease (AD) which is caused by a change in protein structure ✔✔True Alzheimer's disease is caused by aggregation of the Amyloid beta peptide and tangle formation by the tau protein. What kinds of amino acids are likely to drive the formation of these protein aggregates? ✔✔hydrophobic After learning about Alzheimer's disease and one of the drugs used in its treatment, what other drug design strategies could you use to offer treatment for AD? ✔✔1. Drugs that break up the amyloid plaques 2. Drugs that block the production of amyloid beta peptide 3. drugs that inhibits the aggregation of protein structures A substrate binds to an enzyme at a specific site is referred to as ✔✔an active site You are in charge of designing a drug that inhibits the activity of a specific enzyme. An important criteria for the drug selection is to ensure that the drug is directly in competition with the original substrate when binding to the active site of the enzyme. What inhibitor would be an ideal choice? ✔✔A competitive inhibitor These factors can affect the protein folding and activity of an enzyme: ✔✔1. pH 2. Heat 3. Reducing agents One way a cell can avoid overproduction of a molecule is by using a particular type of inhibition in which the molecule itself acts as an inhibitor for an enzyme in its production pathway. This type of regulation is known as feedback inhibition ✔✔True What type of enzyme adds a phosphate to another molecule? ✔✔Kinase What are possible effects that phosphorylation/dephosphorylation can have on the activity of an enzyme? ✔✔1. turn the enzyme on 2. turn the enzyme off In the enzymatic cycle, the enzyme shape is changed when substrate binds and resumes its original shape when product is released after substrate is converted to product. ✔✔True An enzyme increases the rate of a chemical reaction by: ✔✔decreasing the activation energy Compared to a patient that is not on a statin medication, In a patient taking a statin medication the concentration of cholesterol would decrease, the concentration of HMG-CoA would increase, and the concentration of Acetoacetyle CoA would stay the same ✔✔True Primary structure consists of the order of amino acids in a protein. These are held together with peptide bonds that are formed by a dehydration reaction. ✔✔True What types of chain interaction stabilize the tertiary structure of proteins, including: ✔✔1. ion pairs 2. hydrophobic interactions 3. hydrogen bonds 4. disulfide bonds Secondary structure of proteins ✔✔1. It includes beta pleated sheets as a common form 2. it includes alpha helices as a common form 3. it involves hydrogen bonding between the backbone atoms In order to fulfill their function, proteins must fold in proper, 3-D conformations, which molecules, available in a cell, is likely to help a protein fold properly? ✔✔chaperone A misfolded protein can: ✔✔1. can protein aggregation 2. lose normal function 3. can be degraded by the cell 4. can be the result of denaturation True about the different levels of protein structure: ✔✔1. The interactions between the R groups of the amino acids make up the tertiary level structure of a protein 2. Peptide bonds between amino acids make up the primary structure of a protein 3. Two or more polypeptides each with their own secondary structure and tertiary structures come together to form a single larger quaternary structure of a protein The role that protein structure can play in the disease process: ✔✔Mutation of an active amino acid changes an enzymes ability to bind a substrate Aggregation of the proteins is the main reason behind many neurodegenerative diseases. What mutations will likely cause a neurodegenerative disease? ✔✔Replacing a polar amino acid with a non polar amino acid Which pair (protein and technique) will likely denature a protein? ✔✔Hydrogen bond