DNA-RNA Amino Acid Protein

In this chapter we discuss DNA-RNA Amino Acid Protein.

DNA is a type of _____________

nucleic acid

__________ are found in virtually all cells

Nucleic acids

What is the function of nucleic acids?

To encode heritable information and pass it on from generation to generation

What three things make up nucleotides?

Phosphate, pentose sugar, and pyrimidine or purine base

What are the four bases in DNA?

Adenine, guanine, cytosine, and thymine

What are the four bases in RNA?

Adenine, guanine, cytosine, and uracil

How many strands does RNA have? DNA?

RNA is a single strand, DNA is double

Which base pairs with Adenine?


Which base pairs with Guanine?


Where is DNA located?

In the Nucleus

What encases the DNA?


How many chromosomes do humans have?

46. 23 pairs


Small segment of DNA that contains all the pairs of chromosomes

When was the double helix discovered?


Who began the Human Genome project?

Francis S Collins

Hereditary information is stored in ______


The individual building blocks of DNA are called


A DNA molecule consists of two nucleotide strands twisted into a

double helix

The ___________ of the DNA stands pair in a consistent fashion.


What is the RNA transcription for the DNA strand 5- GCT ATG CAT CGT – 3


Which template DNA sequence would the short transcript 5- AUC CGU ACG -3 be derived from?


What is the complementary sequence for the following DNA sequence? 5- GCC ATC TCG AAT -3


Assuming 100% reaction efficiency, how many DNA copies are created after the completion of four complete PCR cycles?


What is the function of DNA polymerase in the process of PCR?

It recognizes the primers and uses the available dNTPs to replicate the template DNA sequence

What type of mutation occurs when cytosine is completely mutated to guanin in the DNA sequence?


When using heat to denature a protein, which force is the first to be disrupted as temperature increases?

Hydrophobic interactions

Which term describes the order of amino acids in a peptide chain?

Primary structure

A commonly used technique for protein denaturation is adding an acid or a base to dramatically change the pH.

Which force is most impacted by this change in pH?

hydrophobic interactions

In which situation could a body function be disrupted by altering protein structure?

A mutation in aconitase blocks an essential step in aerobic metabolism

How can an alteration in protein structure lead to a disease state?

A mutation replaces an isoleucine with an aspartic acid in a transcription factor protein, which blocks the normal folding of the protein and its function in the expression of certain genes.

Which structural level shows the greatest difference when comparing denatured proteins with the normal version of the protein?


Frying an egg changes the egg white from a clear liquid to an opaque solid.

Which molecular change in the albumin protein causes this change in appearance?

Hydrophobic interactions form between denatured egg white proteins.

What is the driving mechanism of plaque formation in prion diseases?

Propagation of misfolding from one protein to another

Which feature of a protein made of a single polypeptide chain is most directly responsible for its function?

Three-dimensional structure

How does the Bohr effect describe the relationship between carbon dioxide levels, blood pH and the amount of oxygen bound to hemoglobin?

An increase in carbon dioxide production leads to a decrease in blood pH, causing hemoglobin to release oxygen more readily.

Which statement describes the binding of oxygen gas to a heme group?

The binding of oxygen gas to heme changes the structure of the heme group.

Which characteristic of myoglobin makes it an effective oxygen storage molecule?

It has a high affinity for oxygen.

At low O 2 concentrations, how does myoglobin’s affinity for O 2 relate to hemoglobin’s affinity for O 2?

Myoglobin has a much greater affinity for O 2 than hemoglobin does.

How does pH level promote the deoxygenated conformation of hemoglobin?

When pH lowers, excess H + binds to negatively charged side chains on hemoglobin and changes ionic bonds between subunits to favor the T-state

What is occurring in surrounding tissues as the amount of hemoglobin saturated with oxygen increases?

The amount of carbon dioxide decreases.

What is feedback inhibition?

Reversible, noncompetitive inhibition of an enzyme in a pathway by a product of that pathway

Which form of enzyme regulation is likely to be used by an organism to control the catalytic activity of its enzymes as it adapts to changes in available nutrients?

Feedback inhibition

How does heating beyond optimum temperature inactivate enzymes?

By changing the enzyme’s three-dimensional shape

What occurs in enzymes during the phenomenon of induced fit?

Substrate binding causes a conformational change.

Which portion of the enzyme does the substrate bind to?

Active site

Which type of inhibition occurs when a particular drug binds to the allosteric site of an enzyme and subsequently changes the enzyme’s structure?


What occurs immediately after the appropriate molecule enters the active site of an enzyme?

The enzyme binds the molecule to form an enzyme-molecule complex.

How is energy provided for ATP production during the final stage of aerobic metabolism?

Protons diffuse through a transmembrane protein.

What occurs in an otherwise healthy person whose diet has very few carbohydrates and high levels of fats?

Acetone is produced in the blood.

Which event is stimulated by release of glucagon into the blood?

Increase in lipolysis of triglycerides

What are the possible blood types of the parents of a patient with blood type AB?

A and B

Oxidative damage to DNA can often result in the alteration of a single nucleotide. Which DNA repair mechanism would repair this type of damage?

Base excision repair

Xeroderma pigmentosum (XP) is a recessive genetic disease that occurs when one or more of the genes that perform nucleotide excision repair are nonfunctional. Why do XP patients have a much higher incidence of skin cancer than the general population?

The mutation rate of all other genes is higher due to failure to repair.

Which reaction is responsible for the formation of polypeptides?


Which amino acid R group is charged?

The one with a pos or neg charge

Which amino acid R group is polar?

Non charged with Oxygen or Nitrogen

Which amino acid R group is nonpolar?

Non charged without Oxygen or Nitrogen

Which amino acid R group makes disulfide bonds?

A non polar amino acid with Cysteine (S)

Which amino acid R group makes ionic bonds?


What type of bond does a charged amino acid make?

Ionic bond

Which amino acid R group makes a disulfide bond?

A nonpolar with a Cysteine (S)

How does insulin impact carbohydrate metabolism?

It stimulates the uptake of glucose from the blood by cells in the body

How does insulin reduce blood glucose levels?

It increases the translocation of GluT4 transporters to the cell membrane

Approximately how many ATP molecules can be produced from a single molecule of glucose during aerobic metabolism


Which cellular condition prompts the cell to perform fermentation rather than the Krebs cycle?

Lack of O2

Which causes the symptoms of noninsulin-dependent (Type 2) diabetes?

There are not enough GluT4 transporters on plasma membranes

Which metabolic pathway involves coenzyme A, NAD, and FAD?

Beta Oxidation

Which molecule is pyruvate directly converted to under aerobic conditions?


How many molecules of lactate are required to produce one molecule of glucose


What is the role of oxygen in aerobic metabolism?

It acts as the final electron acceptor in the electron transport chain

Which pathway is triggered by increasing levels of epinephrine and provides a quick increase in available glucose?


Which type of molecule can be used in gluconeogenesis?

Amino acid

Which molecule acts as the primary signal for glycogen breakdown?


What is a possible chemical formula for a momounsaturated fatty acid?


What is the function of the class of lipids known as eicosanoids?

They act as signaling molecules

What is a glycolipid?

A Polymer of monosaccharides covalently attached to a membrane lipid

Which component of red blood cells determines blood type in the ABO blood group system?

glycolipids and glycoproteins

Which vitamin is not absorbed by phospholipid micelles?

Vitamin C

What occurs during the process of alternative splicing of mRNA?

Alternate combinations of exons within the same gene are linked together

Which type of mammalian DNA damage repair requires the presence of the chromosome that is homologous to the damaged chromosome?


How many peptide bonds are present in a dipeptide?


Which force is most influential in determining the tertiary structure of a protein?

Hydrophobic effect

What is the name of large, functional protein structures composed of smaller proteins with multiple subunits?

Quaternary structure

Pepsin, the enzyme that catalyzes the breaking of peptide bonds, has the highest activity in the acidic environment of the stomach. what process is disrupted after a patient ingests excessive antacid that neutralizes the pH of the stomach?

Protein catabolism

In which situation could a body function be disrupted by altering protein structure?

A mutation in collagen results in weak bones

How can protein function be altered or lost in a disease state?

A deficiency of a specific metal ion inhibits an enzyme because it is required for its catalytic mechanism

Which structural level shows the greatest difference when comparing denatured proteins with the normal version of the protein?


Which level of protein structure is established through the dehydration synthesis of peptide bonds?


Which situation would most likely lead to a permanent alteration of protein function?

A mutation that substitutes a hydrophobic amino acid with a hydrophilic amino acid

Identify the factors that favor the oxygenated form of hemoglobin

High pH, low carbon dioxide

Which metal ion is bound to the porphyrin ring in hemoglobin?


In what condition does hemoglobin bind to oxygen most readily?

Hemoglobin is already bound to one oxygen molecule

Which feature of hemoglobin makes it an effective oxygen transport molecule?

Its affinity for oxygen is regulated by pH

How does hemoglobin keep blood pH neutral during exercise?

Deoxygenated hemoglobin binds to excess H

What is a temporary modification to protein structure by kinases that alters enzyme function?


Which enzyme binding scenario best describes enzyme specificity and action?

An enzyme binds one substrate or closely related substrates to catalyze only one reaction.

Which change will likely increase the activity of an enzyme currently at optimal conditions?

Significantly increasing substrate concentration

Acetylcholine is broken down to acetate and choline by an enzyme calledacetylcholinesterase. Low levels of acetylcholine in the brain is associated with neurodegenerative disease. Which of the following medications could be used to treat neurodegeneration associated with low acetylcholine levels?

Noncompetitive inhibition

What stimulates beta-oxidation of fatty acids?

An increase in NAD concentration in the mitochondrial matrix

What is a function of cholesterol?

Maintains membrane fluidity

How would lipid production in a cell change in order to maintain fluidity of its cell membrane as it adapts to lower temperatures?

Produce lipids with shorter fatty acid chains.

How many ATP molecules are used in the conversion of pyruvate to glucose?


Long-distance runners often consume energy gels that are high in carbohydrates during their run. Which pathway is triggered by the intake of carbohydrates during exercise?


Which cellular organelle required for the citric acid cycle and electron transport chain is not present in red blood cells?


How would a genetic condition that inhibits the breakdown of glucose impact metabolism?

Activates glycogenesis

Where does substrate-level phosphorylation occur in the following metabolic pathway?

Step 3

What occurs during the biochemical process of glycation?

A covalent bond forms between a sugar and a protein or lipid.

Which complex polysaccharide acts as an energy-storing molecule in the liver?


Which components are involved in translation?

mRNA, tRNA, ribosome

What direction does DNA polymerase synthesize new DNA strands?

5 to 3

Which DNA repair mechanisms can fix the damage done by UV radiation in the form of thymine dimers?

nucleotide excision repair

What molecule fuels the activity of our bodies?


What are the three major steps in aerobic metabolism?

Glycolysis, Krebs cycle, and electron transport chain (ETC)

What are needed as inputs for the overall process of cellular respiration?

Sugar, oxygen

What are the outputs of cellular respiration?

ATP, carbon dioxide, water

How many molecules of ATP are produced per molecule of glucose during aerobic metabolism?


C6H12O6 is what molecule?


Where does glycolysis take place?


What is glycolysis?

breaking down glucose

What is breaking down glucose called?


What are the inputs for glycolysis?

Glucose, 2 ATP, 4 ADP, and 2 NAD+

What is glucose converted to during glycolysis?


Where does the krebs cycle occur?

the matrix

What are the inputs for the krebs cycle?

Acetyl CoA, NAD+, FAD, and GDP

What are the outputs from the Krebs cycle?


What are the inputs for ETC?

NADH, FADH2, O2, Pi, and ADP

What are the outputs for ETC?

NAD+, FAD, H2O, and ATP

Where does ETC take place?

Inner membrane

What must be present in order for pyruvate to enter the matrix and start the Krebs cycle?


What does pyruvate convert into to start the krebs cycle?

Acetyl CoA

During the ETC what is transferred through to the intermembrane space by the NAD and FAD?


What is transferred back into the matrix during ETC from NAD and FAD?


What allows the protons to move back into the matrix?

The ATP synthase

What is caused by the protons moving back into the Matrix


What happens to NADH when it gives up a proton?

It becomes NAD+

What happens when Oxygen is not present?

The ETC cannot occur

What are the steps of anaerobic metabolism

Glycolysis, fermentation

When does the body use anaerobic metabolism?

When there is no oxygen available, like during exercise

What is glycogen?

A chain of glucose

What is the process of making glycogen?


What is the function of glucagon?

It tells your body to release glycogen back into the blood stream when glucose levels are low

What is the process of breaking glycogen back into glucose?


Putting molecules together in chains is called ———–.


Breaking the chains back into individual molecules is called _________


A chain of fatty acids is called __________


Fatty acids form triglycerides through which process?


Triglycerides are broke back into fatty acids during which process?


Amino acids bind together in a chain to form ______.


Amino acids form proteins through which process?

Dehydration synthesis

Proteins are broke down into amino acids during which process?

Hydrolytic cleavage

What is a glycated protein?

Glucose + protein

What causes neuropathy in DM?

AGEs stick to the walls of the vessels and inhibit circulation

How many carbons does each acetyl-CoA have?


How do you determine how many rounds of beta oxidation are needed?

Divide the total number of carbons by 2, then subtract one.

What type of bonds hold the amino acid together?

Peptid bonds

Which structure is the R group interactions?


What can disrupt a hydrophobic interaction?

Increase temperature

What can disrupt a hydrogen bond?

Increase temperature or change in pH

What can disrupt an ionic bond?

Change in pH or adding salt