DNA-RNA Amino Acid Protein Blood pH

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?

Thymine


Which base pairs with Guanine?

Cytosine


Where is DNA located?

In the Nucleus


What encases the DNA?

Chromosomes


How many chromosomes do humans have?

46. 23 pairs


Gene

Small segment of DNA that contains all the pairs of chromosomes


When was the double helix discovered?

1953


Who began the Human Genome project?

Francis S Collins


Hereditary information is stored in ______

DNA


The individual building blocks of DNA are called

Nucleotides


A DNA molecule consists of two nucleotide strands twisted into a

double helix


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

Bases


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

5 – ACG AUG CAU AGC – 3


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

5- CGT ACG GAT -3


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

5- ATT CGA GAT GGC -3


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

16


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?

Nonsense


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?

Tertiary


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?

Irreversible


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?

Dehydration


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?

Charged


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

30


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?

Acetyl-CoA


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

2


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?

glycogenolysis


Which type of molecule can be used in gluconeogenesis?

Amino acid


Which molecule acts as the primary signal for glycogen breakdown?

glucagon


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

C8H14O2


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?

Recombination


How many peptide bonds are present in a dipeptide?

1


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?

Tertiary


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

primary


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?

Iron


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?

Phosphorylation


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?

6


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?

Glycolysis


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

Mitochondria


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?

Glycogen


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?

ATP


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?

30


C6H12O6 is what molecule?

Glucose


Where does glycolysis take place?

cytoplasm


What is glycolysis?

breaking down glucose


What is breaking down glucose called?

Glycolysis


What are the inputs for glycolysis?

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


What is glucose converted to during glycolysis?

Pyruvate


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?

CO2, NADH, FADH2, and GTP


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?

Oxygen


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?

H+


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

H20


What allows the protons to move back into the matrix?

The ATP synthase


What is caused by the protons moving back into the Matrix

ATP


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?

Glycogenesis


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?

Glycogenolysis


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

Anabolism


Breaking the chains back into individual molecules is called _________

Catabolism


A chain of fatty acids is called __________

Triglyceride


Fatty acids form triglycerides through which process?

Lipogenesis


Triglycerides are broke back into fatty acids during which process?

Lipolysis


Amino acids bind together in a chain to form ______.

Protein


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?

2


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?

Tertiary


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


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