BRAINSCAPE GAG Flashcards
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Hydroxyl
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Carbonyl
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Carboxyl
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Amino
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Sulfhydryl
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Phosphate
Properties: Hydroxyl
polar
Properties: Carbonyl
polar
Properties: Carboxyl
polar, acidic
Properties: Amino
polar, basic
Properties: Sulfhydryl
slightly polar
Properties: Phosphate
polar
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Ionized Phosphate
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Ionized Carboxyl
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Ionized Amino
Definition: Monomer
The smallest repeating unit of a polymer
Definition: Polymer
A large molecule composed of repeating monomers
Definition: Monosaccharide
A simple sugar; a carbohydrate composed of 3-7 carbon atoms
Definition: Disaccharide
A carbohydrate composed of two monosaccharides joined by a covalent bond
Definition: Polysaccharide
A carbohydrate polymer composed of many monosaccharides joined by covalent bonds
Definition: Glycosidic Linkage
A covalent bond between monosaccharides
Formula: Glucose/Fructose/Galactose
C6H12O6
Compare: Alpha Glucose vs Beta Glucose
Alpha glucose has a hydroxyl in the down position on its first carbon, beta has a hydroxyl in the up position
Compare: Glucose vs Galactose
Glucose has a hydroxyl in the down position on its fourth carbon, galactose has one in the up position
Which reaction releases a water molecule?
Dehydration synthesis/condensation
Which reaction uses up a water molecule?
Hydrolysis reaction
What is maltose made of?
Alpha Glucose + Alpha Glucose
What is sucrose made of?
Alpha Glucose + Beta Fructose
What is lactose made of?
Beta Glucose + Beta Galactose
Which carbons link in the formation of maltose?
alpha 1:4 linkage
Which carbons link in the formation of sucrose?
alpha 1:2 linkage
Which carbons link in the formation of lactose?
beta 1:4 linkage
Rank the three common polysaccharides from least branched to most branched
Cellulose, starch, glycogen
What is the use of glycogen?
Short-term energy storage in animals
What is the use of starch?
Short-term energy storage in plants
What is the use of cellulose?
Structural support in plants
How often does glycogen branch?
Approximately every ten residues
How often does starch branch, and where?
Approximately every 30 residues, in the amylopectin
Which carbons link in cellulose, and of which monomer?
1:4 beta glucose linkage
What is chitin made of?
A carbohydrate with a nitrogen-containing functional group
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Alpha glucose
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Galactose
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Fructose
Which carbons link in glycogen, and of which monomer?
alpha glucose 1:4 linkage
Which carbons link in amylopectin, and of which monomer?
alpha glucose 1:4 linkage
Which carbons link in branches, and of which monomer?
alpha glucose 1:6 linkage
Functions: Triglycerides
long-term energy storage, twice the energy per grams compared to carbohydrates/proteins, provide insulation, components of cell membranes
Features: Saturated Fatty Acids
no double bonds, saturates with hydrogen atoms, straight chain, solid at room temperature
Features: Unsaturated Fatty Acids
One or more double bonds, not saturated with hydrogen atoms, liquid at room temperature
Features: Cis Fats
Very bulky, liquid at room temperature
Features: Trans Fats
Pack together, solid at room temperature, unhealthy
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Glycerol
<img></img><br></br><br></br>Is this saturated or unsaturated?
Saturated
<img></img><br></br><br></br>Is this saturated or unsaturated?
Unsaturated
What are the two main types of linkages?
Ester linkages and ether/glycodic linkages
How many water molecules are produced during the creation of triglyceride?
Three
<img></img><br></br><br></br>What type of linkage is this?
Ester linkage
<img></img><br></br><br></br>What type of linkage is this?
Ether linkage
Definition: Valence
The number of chemical bonds that each atom of a chemical element typically form
What is the valence of: Carbon, Oxygen, Phosphorus, Nitrogen, Sulphur, Hydrogen?
4/2/5/3/2/1
Definition: Isotope
Atoms with the same number of protons but a different number of neutrons
Definition: Radioisotope
An unstable isotope that emits radiation and decays over time while becoming more stable
How are radioisotopes used in medicine?
Radioisotope tracing, a process where radioactive material is injected into the body and traced using a positron emission topography (PET) scan to locate tissues with higher levels of activity (higher activity indicates cancer)
Definition: Biochemistry
The study of the chemical processes within living organisms
Definition: Intramolecular Forces
The forces that hold atoms together within a molecule
Definition: Intermolecular Forces
The attractive and repulsive forces between the molecules of a substance
Definition: Electronegativity
The tendency of a nucleus to attract electrons towards itself
An electronegativity difference of less than __ results in a(n) __ bond
0.5, pure covalent
An electronegativity difference between __ and __ results in a(n) __ bond
0.5, 1.6, polar covalent
An electronegativity difference greater than __ results in a(n) __ bond
1.6, ionic
Definition: Hydrogen Bonding
The attraction of a slightly positively charged hydrogen atom to a slightly negatively charged oxygen, nitrogen or fluorine atom that is also connected to a hydrogen atom
Definition: Hydrophobic
Does not dissolve in water
Definition: Hydrophillic
Dissolves in water
Why is water described as polar?
The two hydrogen atoms have slightly positive charges while the oxygen atom has a slightly negative charge due to their electronegativity difference
State the 4 unique properties of water
Hydrogen bonding, special density properties, polarity, dissociation of intramolecular bonds
What property of water explains how water can travel within the xylem vessels of a tree?
Hydrogen bonding, more specifically cohesion/adhesion. Cohesion making the water molecules stick together, and adhesion making them stick to the xylem.
What property of water explains how belly flops hurt?
Hydrogen bonding, more specifically surface tension
What is surface tension?
The tension of the surface of a liquid caused by the attraction of the molecules on the surface to the bulk of the liquid.
What property of water explains how drinking lots of fluids can help reduce a fever?
Hydrogen bonding, more specifically water’s high specific heat capacity, which is explained by the high amount of energy needed to break these bonds, meaning it takes a lot of heat to make water molecules move faster and heat up
What property of water explains why lakes freeze from the top down?
Water becomes less dense as a solid, which causes ice to float to the top
What property of water explains how the products of digestion easily diffuse across the villi membrane?
Water’s polar nature makes it a solvent, dissolving the products of digestion, making it easier for them to diffuse as non-solids
Definition: Acid
Acids are substances with high concentrations of H+ ions. They donate protons, and they produce H+ ions when dissolved in water.
Definition: Base
Bases are substances with low concentrations of H+ ions. They accept protons, and they produce OH- ions when dissolved in water.
Definition: Buffer
A solution that resists changes in pH when an acid or base is added to it
Why are buffers important to biological systems?
They maintain acid-base homeostasis by releasing H+ or OH- ions. This prevents complications that can occur if the pH of the body is too high or too low
Formula: Maltose/Sucrose/Lactose
C12H22O11
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Phospholipid
What are the main component of cell membranes?
Phospholipids
Definition: Phospholipid
A lipid with a hydrophillic “head” and a hydrophobic “tail”
What is the structural difference between a triglyceride and a phospholipid?
One fatty acid is replaced with a phosphate group
Definition: Phospholipid Bilayer
A thin polar membrane formed in aqueous environments that allows for the cell to be selectively permeable
Definition: Steroids
Hydrophobic molecules composed of four linked carbon rings
Functions: Steroids
component of cell membrane in animals, sex hormones, used to reduce inflammation
Definition: Waxes
Diverse structures, solid at room temperature. Most have long chains of fatty acids or carbon rings.
Example: A wax produced in plants
Carnauba wax
Example: A wax produced in animals
Beeswax, earwax
Functions: Waxes
Hydrophobic, waterproof protection
What are protein monomers called?
Amino Acids
What bond is present in proteins?
Peptide bond
What are protein polymers called?
Polypeptides
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Amino Acid
Definition: Zwitterion
A molecule that contains an equal amount of positively or negatively charged functional groups
Visualize: Peptide Bond
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__ structure is the linear sequence of amino acids
primary
__ structure is the amino acids hydrogen bonding and either forming coils or folds
Secondary
What are the two secondary structures of proteins?
Alpha helix and beta pleated sheets
What do helixes and sheets in a polypeptide arrange themselves by in tertiary structures?
Hydrophobic/philicness, hydrogen bonding, electrostatic charges and molecular chaperones
__ structure is when various polypeptides join together to form multi-polypeptide proteins
Quaternary
How are alpha helixes created?
Hydrogen bonding between every fourth amino acid within a strand
Example: Alpha helix
In keratin
How are beta pleated sheets created?
Hydrogen bonds forming between two parts of the polypeptide chain layered on each other
Example: Beta pleated sheet
Inside spider webs
R-group interactions create __ structure
Tertiary
Definition: Denaturation
The breaking of stabilizing bonds within a protein molecule that disrupt its shape
What causes denaturation?
Changes in pH, heat, exposure to alcohol, high salt concentrations
What are are nucleic acid monomers called?
Nucleotides
What is a sugar-phosphate backbone made of?
Nucleotides bonded by phosphodiester bonds
What are the two types of nucleic acids?
Deoxyribonucleic acid (DNA) and ribonucleic acid (RNA)
How do DNA and RNA differ in their sugars?
RNA contains Ribose, a sugar with 5 oxygens, while DNA contains deoxyribose, a sugar with 4 oxygens (lacking one on the second carbon)
What is DNA’s purpose?
It contains the genetic information of organisms, which are decoded into the particular amino acid sequences of proteins
What is RNA’s purpose?
It contains the genetic information for some virus particles, and it assists DNA to make proteins
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Deoxyribose
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Ribose
What is a nucleotide made of?
A sugar, a nitrogenous base and a phosphate group
What are the two pairs of nitrogenous bases in DNA
Adenine and Thymine; Guanine and Cytosine
What are the two pairs of nitrogenous bases in RNA
Adenine and Uracil; Guanine and Cytosine
List the purines of DNA and RNA
Adenine and Guanine
List the pyrimidines of DNA and RNA
Thymine, Uracil, and Cytosine
How many hydrogen bonds are present in Guanine-Cytosine pairings?
Three
How many hydrogen bonds are present in Adenine-Thymine pairings?
2
Definition: Enzyme
A protein with catalytic purposes due to its power of specific activation
Enzymes have a __ shape
Globular
How much faster do enzymes allow reactions to occur?
10^6 times faster
What is the active site?
A specifically shaped site on an enzyme with a unique chemical environment that permits a chemical reaction to proceed more easily
What is activation energy?
The energy that chemical reactions need to begin
What state are molecules in during the initial input of energy?
Transition state
Why are enzymes necessary instead of just raising body temperature?
Biological systems are very sensitive to temperature changes
How do enzymes increase the rate of reactions?
They lower the activation energy
Definition: Cofactor
A metal ion or mineral that is needed by some enzymes to help the reaction
Definition: Coenzymes
Organic molecules/vitamins that assist the reaction
Definition: Substrate
The reactants activated by the enzyme, specific to an enzyme
The __ cycle refers to the lock and key mechanism
Catalytic
__ may be used more than once
Enzymes
What is the induced fit hypothesis?
When a substrate combines with an enzyme it changes the active site in order to create a precise conformation. Reduces activation energy by stretching the bonds of the substrate.
__ enzymes catalyze hydrolysis reactions
Hydrolase
What are some factors that affect enzymes?
Substrate concentration, pH, temperature, and inhibitors
How does substrate concentration affect enzymatic reactions?
The reaction velocity increases as substrates become more concentrated, but when all enzyme molecules are occupied this velocity reaches a maximum.
How does enzyme concentration affect enzymatic reactions?
As enzymes become more concentrated, more enzymes are available to bind with substrates, increasing the maximum reaction velocity.
__ are chemicals that reduce the rate of enzymatic reactions
Inhibitors
What is competitive inhibition?
Inhibitors that resemble the substrate compete with the substrate for the active site. If more inhibitor is present compared to substrate it will successfully bind with the active site.
What is non-competitive inhibition?
Inhibitors bind to the allosteric site, which regulates enzyme activity. They prevent the enzyme from working.
What is negative feedback in biochemical pathways?
The last reaction of a pathway produces a non-competitive inhibitor that prevents the enzyme that started the pathway from working again, ensuring cell products are not produces unnecessarily.
Rank the three proteins used in the Proteins Lab by how sensitive they were to HCl
Albumin, Casein, Gelatin
How do strong acids and bases affect protein denaturation and solubility?
They both denature proteins due to their extreme placement on the pH spectrum, lowering solubility and producing a precipitate
Which metal salt (CuSO4 and AgNO3) caused the most albumin denaturation in the Proteins Lab?
AgNO3 showed a stronger denaturing effect due to the fact that silver salts are more toxic than copper salts
Does isopropyl alcohol work well as a disinfectant? Why or why not?
Yes, it denatures the proteins in bacteria as proven by the fact that it made albumin clear and transparent.
Why is heat an effective form of sterilization?
Heat effectively denatures proteins, which are present in bacteria.
How does heat affect enzyme activity?
It weakens the hydrogen bonds within the enzyme by increasing their movement, causing the enzyme to lose its shape and ability to function properly.
How does cold affect enzymatic activity?
The cold slows down the movement of molecules which results in less collisions, and it renders the bonds within the enzyme inflexible which does not let the subtrate bind properly.
How does pH affect enzymatic activity?
Enzyme active sites are denatured when not in optimal pH levels which slows reaction rate
How do acids and bases specifically affect hydrogen bonds?
Excess H+ ions bond with negatively charged carboxyl groups, and OH- ions remove H+ from positvely charged amino groups.
How does enzyme surface area affect enzymatic activity?
If enzyme surface area is larger, the substrates can interact with more active sites.
Definition: Isoelectric Point
The pH at which a molecule has no electrical charge
What happens to solubility at the isoeletric point?
At the isoelectric point a molecule is at its minimum solubility because there is no polarity repelling it or attracting it to other particles in its environment.
Describe the first step of glycolysis in detail
Glucose converted into glucose 6-phosphate by a hexokinase. This adds a phosphate group to glucose’s sixth carbon. This uses 1 ATP. This is irreversible.
Describe the second step of glycolysis in detail
Glucose 6-phosphate converted into fructose 6-phosphate by an isomerase. This is reversible.
Describe the third step of glycolysis in detail
Fructose 6-phosphate converted into fructose 1,6-bisphosphate by a kinase. This adds a phosphate group to fructose 6-phosphate’s first carbon. This uses 1 ATP. This is irreversible.
Describe the fourth step of glycolysis in detail
Fructose 1,6-bisphosphate converted into dihydroxyacetone phosphate (DHAP) and glyceraldehyde 3-phosphate (G3P) by aldolase. This is reversible.
Describe the fifth step of glycolysis in detail
Dihydroxyacetone phosphate (DHAP) is converted into glyceraldehyde 3-phosphate (G3P) by an isomerase. Glyceraldehyde 3-phosphate can also be turned into dihydroxyacetone phosphate by this isomerase, but that is not important in glycolysis. This is reversible.
Describe the sixth step of glycolysis in detail
Both glyceraldehyde 3-phosphates (G3P) are oxidized into 1,3-bisphosphoglycerates by glyceraldehyde 3-phosphate dehydrogenases. Two redox reactions occur during this step, with NAD+ being reduced into NADH and H+. It also adds an inorganic phosphate (no ATP spent) to each glyceraldehyde 3-phosphate. This is reversible.
Describe the seventh step of glycolysis in detail
Both 1,3-bisphosphoglycerates are converted into 3-phosphoglycerates by a kinase. This removes a phosphate, and adds it to ADP, producing 1 ATP (actually two). This is reversible.<br></br><br></br>
Describe the eighth step of glycolysis in detail
Both 3-phosphoglycerates are converted into 2-phosphoglycerates by a mutase. This moves the phosphate from the 3rd carbon to the 2nd carbon. This is reversible.
Describe the ninth step of glycolysis in detail
Both 2-phosphoglycerates are converted into phosphoenolpyruvates by enolase. This releases a water molecule. This is reversible.
Describe the tenth step of glycolysis in detail
Both phosphoenolpyruvates are converted into pyruvates by a kinase. This removes the phosphate, and adds it to ADP, producing 1 ATP (actually two). This is irreversible.
Function: Kinase
Adds a phosphate group to a molecule
Function: Dehydrogenases
Catalyze oxidations by transferring hydrogen
Function: Isomerases
Alter the physical structure of molecules
Function: Mutases
Isomerases that rearrange functional groups
What is the net reaction of glycolysis?
Glucose + 2ADP + 2Pi + 2NAD+ –> 2 Pyruvate + 2 ATP + 2 NADH + 2H2O
What is the net reaction of pyruvate oxidation?
1 Pyruvate + NAD+ + HS-CoA -> 1 Acetyl-CoA + NADH + H+ + CO2
Formula: Cellular respiration
C6H12O6 + 6O2 –> 6CO2 + 6H2O + ATP
Describe the first step of the Krebs cycle in detail
Acetyl-CoA (2C) and oxaloacetate (4C) are fused into citrate (6C) by citrate synthetase. This releases the CoA.
Describe the second and third steps of the Krebs cycle in detail
Citrate (6C) is rearranged into isocitrate (6C) by aconitase.
Describe the fourth step of the Krebs Cycle in detail?
Isocitrate (6C) is rearranged is converted into alpha-ketoglutarate (5C) by isocitrate dehydrogenase. 1 CO2 is released. NAD + is converted to NADH and H+.
Describe the fifth step of the Krebs cycle in detail
Alpha-ketoglutarate (5C) is converted into succinyl-CoA (4C) by alpha-ketoglutarate dehydrogenase. 1 CO2 is released. NAD + is converted to NADH and H+. CoA gets added to the molecule.
Describe the sixth step of the Krebs cycle in detail
Succinyl-CoA (4C) is converted into succinate (4C) by succinyl-CoA synthetase. It also creates GTP from GDP + inorganic phosphate. GTP lends a phosphate to ADP to produce 1 ATP. The CoA is released.
Describe the seventh step of the Krebs cycle in detail
Succinate (4C) is converted into fumarate (4C) by succinate dehydrogenase. FAD is covnerted into FADH2.
Describe the eighth step of the Krebs cycle in detail
Fumarate (4C) is converted into malate (4C) by fumarase. This adds 1 H2O to the molecule.
Describe the ninth step of the Krebs cycle in detail
Malate (4C) is converted into oxaloacetate (4C) by malate dehydrogenase. It also creates NADH and H+ from NAD+.
What enzyme is used in pyruvate oxidation?
Pyruvate dehydrogenase complex
What is the maximum ATP yield of a glucose molecule in a prokaryote?
38 ATP
What is the maximum ATP yield of a glucose molecule in heart, liver and kidney cells?
38 ATP
What is the maximum ATP yield of a glucose molecule in most cells of a eukaryote?
36 ATP
Where does glycolysis take place?
Cytosol
Where does the Krebs cycle take place?
Matrix
Where does oxidative phosphorylation take place?
Mitochondria
Where does pyruvate oxidation take place?
Matrix
What is the H+/ATP ratio in oxidative phosphorylation?
2
How many protons are pumped out of the matrix for each NADH?
6
How many protons are pumped out of the matrix for each FADH2?
4
How many ATP does each NADH make?
3
How many ATP does each FADH2 make?
2
Name the folds of the inner mitochondrial membrane
Cristae
How many carbons does Acetyl-Coa have?
2
What is the waste product of cellular respiration?
CO2