Biochemistry - C785 Module 2
carboxyl group Correct Answer: A -COOH group, found in organic acids.
amino group Correct Answer: a chemical group
... [Show More] consisting of a nitrogen atom bonded to two hydrogen atoms
Where are the hydrophobic amino acids found in the protein? Correct Answer: found in the interior of the protein
What kind of bond connects a positively charged group and a negatively charged group? Correct Answer: ionic bond
What type of reaction forms a peptide bond? Correct Answer: dehydration synthesis
What type of reactions breaks the peptide bond? Correct Answer: Hydrolysis reaction
Peptide bonds are in what structure? Correct Answer: Primary structure
Hydrogen bonds hold which structure together? Correct Answer: Secondary and tertiary
What amino acids are found on the exterior of the protein? Correct Answer: polar amino acids
Two non-polar amino acids make what kind of interaction? Correct Answer: Hydrophobic interactions
Non-covalent interactions between amino acid R groups Correct Answer: hydrophobic, ionic and hydrogen bonds
What structure has a disulfide bond that holds together 2 subunits of an enzyme? Correct Answer: quaternary structure
What structure has an Ionic interactions that hold together 4 different subunits of a protein? Correct Answer: quaternary structure
What structure has an Ionic interactions that hold together 3 identical polypeptides Correct Answer: quaternary structure
non polar amino acids Correct Answer: hydrophobic bond, weak strength, heat disrupts the interaction
primary structure of protein Correct Answer: the amino acid sequence of the polypeptide chain
secondary structure of protein Correct Answer: Hydrogen bonds are involved in this level of structure and the amino and carboxyl groups (backbone) form these bonds
tertiary structure of protein Correct Answer: hydrogen, ionic and disulfide bonds as well as hydrophobic interactions
quaternary structure of a protein Correct Answer: 2 or more polypeptides interact to form the protein
Fate of misfolded proteins Correct Answer: aggregation, degradation and refolding
What kind of interaction between misfolded protein leads to aggregation? Correct Answer: hydrophobic interaction
What kind of proteins take part in the process involving refolding? Correct Answer: chaperones
A diabetic patient is suffering from ketoacidosis has low blood pH. What bond or interaction is most likely to be disrupted within a patient's hemoglobin? Correct Answer: hydrogen bonds and ionic interactions
A patient presents with a fever of 110 F. Which bond or interactions is most likely to be disrupted within a neuronal protein if the fever isn't resolved quickly? Correct Answer: hydrophobic interactions
Frying an egg in a pan changes the egg white color, due to the protein ovalbumin, from translucent to white. Which bond or interaction is most likely to be disrupted within the ovalbumin? Correct Answer: hydrophobic interactions
Protein heated to 140F loss of function and denatured Correct Answer: loss of function and denatured
Native protein misfolds and remains misfolded loss of function and aggregated Correct Answer: loss of function and aggregated
Normally active protein at physiological blood pH, where placed in a solution with a very low pH (less than 2) loss of function and denatured Correct Answer: loss of function and denatured
Protein is placed in a solution with a very high pH (greater than 10) loss of function and denatured Correct Answer: loss of function and denatured
Protein is modified by adding a phosphate group either loss or no loss of function Correct Answer: loss or no loss of function
Composed of amino acids Correct Answer: Proteins, enzymes, cell membrane receptors, antibodies, DNA polymerase
Enzymes are a Correct Answer: special type of protein, so they are also composed of amino acids
When the hydrophobic leucine (CH3) is replaced by the positively-charged arginine (NH2+), the protein will misfold because the amino acids belong to different categories. Correct Answer: A missense mutation in the gene coding for DNA polymerase replaces a leucine in position 44 with an arginine cause the DNA polymerase to misfold
DNA polymerase is responsible for Correct Answer: synthesizing DNA in the DNA replication proess
How many units does hemoglobin have? Correct Answer: Hemoglobin has 4 subunits
Hemoglobin has four subunits. A missense mutation in the gene for hemoglobin causes the subunits to associate improperly and aggregate. What level of protein structure is affected by the mutation that impacts the function of the protein? Correct Answer: Primary structure, cause a change in the amino acid sequence. Quaternary structure because the subunits do not associate properly.
Explain why impacting the structure of hemoglobin affects its function Correct Answer: For hemoglobin, the structure of the protein is important to the protein's ability to bind and release oxygen, which enables our tissues to be oxygenated
Chaperones are Correct Answer: helper proteins that ensure proper protein folding
What is the primary cause of many neurodegenerative diseases? Correct Answer: aggregation
Hydrophobic interactions are disrupted by Correct Answer: temperature(heat)
What type of bonds are disrupted by pH and salt Correct Answer: Ionic bonds and hydrogen bonds
What type of bond is disrupted by reducing agents Correct Answer: Disulfide bonds
Two amino acids are polar, so they would be able to form a ___________________ ______________________ Correct Answer: hydrogen bonds
2 non-polar amino acids make what kind of interaction Correct Answer: hydrophobic interaction
What type of interaction is most likely responsible for the (formation of the aggregate) in Alzheimers and Parkinsons? Correct Answer: Hydrophobic interactions are primarily responsible for the formation of aggregates.
What kind of mutation occurs when a positively charged amino acid is replaced by a hydrophobic amino acid preventing the two subunits from properly interacting Correct Answer: missense mutation
What kind of mutation produces shortened protein that misfolds, aggregates and in eventually degraded Correct Answer: nonsense mutation
Kinase, phosphatase, actin, Peptidase, Insulin are what? Correct Answer: Proteins
Substrate Correct Answer: Molecule that an enzyme will specifically bind to
Activation energy Correct Answer: Energy required to start a reaction
Active site Correct Answer: Substrate-binding site on an enzyme
Catalyst (enzyme) Correct Answer: Substance that speeds up a chemical reaction
Inhibitor Correct Answer: Molecule that stops or slows down an enzyme
Rate of Enzyme-catalyzed reactions Correct Answer: an enzyme increases the rate of the reactions by factors of millions
Describe the enzyme cycle Correct Answer: 1. Enzyme + substrate
2. Enzyme-Substrate complex (Induced Fit)
3. Enzyme-Product complex
4. Enzyme + Product
Examples of Temperature, substrate concentration and pH decrease in enzyme activity Correct Answer: 1. An environment at temperature 37 C
2. A decrease in substrate concentration [Show Less]