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Questions and Answers
What is the chemical reaction that breaks down all the major macromolecules?
What is the chemical reaction that breaks down all the major macromolecules?
Hydrolysis
What is the strongest type of intermolecular bond?
What is the strongest type of intermolecular bond?
Hydrogen bonds
Why is water a liquid at high temperatures?
Why is water a liquid at high temperatures?
Hydrogen bonding holds the water molecules closer together.
What is an amphipathic molecule? Give an example.
What is an amphipathic molecule? Give an example.
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What is a lipid?
What is a lipid?
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What are the 6 major groups of lipids?
What are the 6 major groups of lipids?
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What is the structure of a tri-glyceride?
What is the structure of a tri-glyceride?
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What happens if you add water to an ester group in a tri-glyceride?
What happens if you add water to an ester group in a tri-glyceride?
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What is important to know about the longer carbon chains in a tri-glyceride regarding water solubility?
What is important to know about the longer carbon chains in a tri-glyceride regarding water solubility?
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How soluble are shorter chain fatty acids?
How soluble are shorter chain fatty acids?
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What is special about saturated fatty acids regarding their melting point?
What is special about saturated fatty acids regarding their melting point?
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What is special about unsaturated fatty acids regarding their melting point?
What is special about unsaturated fatty acids regarding their melting point?
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Explain the phospholipids structure.
Explain the phospholipids structure.
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What regions are polar and nonpolar in a membrane?
What regions are polar and nonpolar in a membrane?
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Explain glycolipids structure.
Explain glycolipids structure.
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What do steroids look like?
What do steroids look like?
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How do lipids move through the blood despite being insoluble?
How do lipids move through the blood despite being insoluble?
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What are the major classes of lipoproteins?
What are the major classes of lipoproteins?
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What are proteins made up of?
What are proteins made up of?
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Describe amino acid structure.
Describe amino acid structure.
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What are the basic amino acids?
What are the basic amino acids?
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What are the acidic amino acids?
What are the acidic amino acids?
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What are the nonpolar amino acids?
What are the nonpolar amino acids?
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What is the primary structure of a protein?
What is the primary structure of a protein?
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What is the secondary structure of a protein?
What is the secondary structure of a protein?
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What is the tertiary structure of a protein?
What is the tertiary structure of a protein?
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What is the quaternary structure of a protein?
What is the quaternary structure of a protein?
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What are the five forces that create tertiary structure?
What are the five forces that create tertiary structure?
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What levels of structure are disrupted during the denaturation process?
What levels of structure are disrupted during the denaturation process?
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What is the difference between a proteoglycan and a glycoprotein?
What is the difference between a proteoglycan and a glycoprotein?
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What is the empirical formula for any carbohydrate?
What is the empirical formula for any carbohydrate?
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Describe the chemical structure of glucose.
Describe the chemical structure of glucose.
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Where is glucose stored in alpha linkages?
Where is glucose stored in alpha linkages?
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Who stores glucose with beta linkages?
Who stores glucose with beta linkages?
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What molecule is added to glycogen, starch, and cellulose to break off individual glucose molecules?
What molecule is added to glycogen, starch, and cellulose to break off individual glucose molecules?
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What are the four macromolecules?
What are the four macromolecules?
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What are the three parts of a nucleotide?
What are the three parts of a nucleotide?
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What molecule breaks up nucleic acids into nucleotides?
What molecule breaks up nucleic acids into nucleotides?
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What are some other important nucleotides?
What are some other important nucleotides?
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What are minerals?
What are minerals?
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What are enzymes?
What are enzymes?
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What is activation energy?
What is activation energy?
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An enzyme is typically larger than the substrate.
An enzyme is typically larger than the substrate.
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Where does a substrate attach to an enzyme?
Where does a substrate attach to an enzyme?
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What are the two hypotheses of enzyme and substrate interactions?
What are the two hypotheses of enzyme and substrate interactions?
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One enzyme is tailor-made for one reaction.
One enzyme is tailor-made for one reaction.
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What are saturation kinetics?
What are saturation kinetics?
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What factors affect enzymatic reactions?
What factors affect enzymatic reactions?
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How do cells regulate enzymes?
How do cells regulate enzymes?
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What are the general types of enzyme inhibition?
What are the general types of enzyme inhibition?
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What is feedback inhibition?
What is feedback inhibition?
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What are specific ways in which enzymes are inhibited?
What are specific ways in which enzymes are inhibited?
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What is competitive inhibition?
What is competitive inhibition?
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What is non-competitive inhibition?
What is non-competitive inhibition?
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What is irreversible inhibition?
What is irreversible inhibition?
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What is respiration?
What is respiration?
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Where does glycolysis take place?
Where does glycolysis take place?
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Does glycolysis require oxygen?
Does glycolysis require oxygen?
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Is glycolysis poisoned by oxygen?
Is glycolysis poisoned by oxygen?
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What is the net ATP produced by glycolysis?
What is the net ATP produced by glycolysis?
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What happens to the NADHs at the end of glycolysis if oxygen is not present?
What happens to the NADHs at the end of glycolysis if oxygen is not present?
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If oxygen is present, what happens to the products of glycolysis?
If oxygen is present, what happens to the products of glycolysis?
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What is the energy cost of transporting one NADH into the mitochondria?
What is the energy cost of transporting one NADH into the mitochondria?
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How many ATPs does each NADH produce during the electron transport chain (ETC)?
How many ATPs does each NADH produce during the electron transport chain (ETC)?
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In the mitochondrial matrix, what happens to the pyruvates?
In the mitochondrial matrix, what happens to the pyruvates?
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What are the energetic products of the TCA cycle?
What are the energetic products of the TCA cycle?
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Overall, aerobic respiration of a single glucose molecule results in a net of how many ATPs?
Overall, aerobic respiration of a single glucose molecule results in a net of how many ATPs?
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What is the electron transport chain (ETC)?
What is the electron transport chain (ETC)?
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What is aerobic respiration?
What is aerobic respiration?
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What is the final electron acceptor in the ETC?
What is the final electron acceptor in the ETC?
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How are tri-glycerides burned for energy?
How are tri-glycerides burned for energy?
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How are proteins burned for energy?
How are proteins burned for energy?
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What is the rule of the ratio of gene to polypeptide?
What is the rule of the ratio of gene to polypeptide?
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How many copies of a gene do prokaryotes have?
How many copies of a gene do prokaryotes have?
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For most genes, how many copies do eukaryotes have?
For most genes, how many copies do eukaryotes have?
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What are the three main components of a nucleotide?
What are the three main components of a nucleotide?
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What are the four nitrogenous bases?
What are the four nitrogenous bases?
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What are the four nucleosides?
What are the four nucleosides?
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What is the difference between a nucleotide and a nucleoside?
What is the difference between a nucleotide and a nucleoside?
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What are the purines?
What are the purines?
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What are the pyrimidines?
What are the pyrimidines?
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Which carbon is the PO4 group attached to?
Which carbon is the PO4 group attached to?
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What kind of bond connects the PO4 group to the 3rd carbon on the pentose sugar of the nucleotide chain?
What kind of bond connects the PO4 group to the 3rd carbon on the pentose sugar of the nucleotide chain?
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In a phosphodiester bond, which numbered carbons are connected?
In a phosphodiester bond, which numbered carbons are connected?
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How do the nitrogenous bases bond to each other?
How do the nitrogenous bases bond to each other?
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How many bonds are formed between A and T?
How many bonds are formed between A and T?
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How many bonds are formed between C and G?
How many bonds are formed between C and G?
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Why is replication semi-conservative?
Why is replication semi-conservative?
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In what direction does replication occur?
In what direction does replication occur?
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What enzyme separates the two strands of DNA?
What enzyme separates the two strands of DNA?
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In what direction does DNA polymerase move?
In what direction does DNA polymerase move?
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In what direction does DNA polymerase polymerize the complementary strand?
In what direction does DNA polymerase polymerize the complementary strand?
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In what direction does the replisome move?
In what direction does the replisome move?
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What is the replisome composed of?
What is the replisome composed of?
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Which polymerase polymerizes the leading strand?
Which polymerase polymerizes the leading strand?
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Which polymerase polymerizes the lagging strand?
Which polymerase polymerizes the lagging strand?
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What are Okazaki fragments?
What are Okazaki fragments?
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How does RNA differ from DNA?
How does RNA differ from DNA?
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What are the types of RNA?
What are the types of RNA?
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Where is RNA synthesized?
Where is RNA synthesized?
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Study Notes
Hydrolysis and Macromolecules
- Hydrolysis is the chemical reaction responsible for breaking down major macromolecules into their smaller components.
Inter-molecular Bonds
- Hydrogen bonds are the strongest type of intermolecular bonds, while dipole-dipole and Van der Waals forces are weaker.
Water Characteristics
- Water remains a liquid at high temperatures due to hydrogen bonding, which keeps molecules closely packed.
Ampipathic Molecules
- Ampipathic molecules possess both hydrophobic and hydrophilic regions; example: Phospholipid (hydrophilic phosphate group and hydrophobic lipid tails).
Lipids
- Lipids are biological molecules characterized by low solubility in water, commonly referred to as fats.
Major Groups of Lipids
- Key classes of lipids include:
- Fatty acids
- Triglycerides
- Phospholipids
- Glycolipids
- Steroids
- Terpenes (e.g., pine oils, vitamin A).
Structure of Triglycerides
- Triglycerides consist of a glycerol backbone with three fatty acid chains linked via ester bonds.
Hydrolysis of Triglycerides
- Adding water to triglycerides hydrolyzes ester bonds, yielding glycerol and fatty acids, a reaction accelerated by lipases.
Solubility of Fatty Acids
- Longer carbon chains in triglycerides decrease water solubility due to less significant polar carboxylic groups.
Short vs. Long Chain Fatty Acids
- Short-chain fatty acids exhibit slight water solubility, while longer chains are significantly less soluble.
Saturated vs. Unsaturated Fatty Acids
- Saturated fatty acids contain solely single bonds, resulting in a straight chain and higher melting points due to stronger Van der Waals forces.
- Unsaturated fatty acids have one or more double bonds, yielding a lower melting point and potentially oily consistency at room temperature.
Phospholipids Structure
- Phospholipids have a glycerol backbone, with one carbon attached to a phosphate group and two fatty acid chains, forming a bilayer in cell membranes.
Membrane Regions
- In membranes, polar phosphate regions face outward (hydrophilic), while nonpolar fatty acid chains face inward (hydrophobic).
Glycolipids
- Glycolipids include a glycerol backbone with two fatty acid chains and a carbohydrate attached to one carbon.
Steroids
- Steroids are characterized by slightly amphipathic four-ring structures.
Lipid Transport in Blood
- Lipids are transported in the bloodstream via lipoproteins like HDL and LDL.
Classes of Lipoproteins
- Major lipoprotein classes include:
- Chylomicrons (largest)
- VLDLs (very low density)
- LDLs (low density)
- HDLs (high density and smallest).
Protein Composition
- Proteins consist of one or more polypeptide chains formed by amino acids.
Amino Acid Structure
- Amino acids comprise four components:
- Amino group (NH2)
- R group (20 possible variations)
- Carboxylic acid group (COOH)
- Hydrogen atom.
Basic and Acidic Amino Acids
- Basic amino acids: Histidine, Arginine, Lysine.
- Acidic amino acids: Aspartic acid, Glutamic acid.
Nonpolar Amino Acids
- Nonpolar amino acids include Phenylalanine, Leucine, Tryptophan, Methionine, Glycine, Isoleucine, Valine, Alanine, and Proline.
Protein Structures
- Primary structure: Sequence of amino acids and disulfide bond locations.
- Secondary structure: Includes alpha helices and beta sheets.
- Tertiary structure: 3D shape formed by folding.
- Quaternary structure: Assembly of multiple polypeptide chains.
Forces in Tertiary Structure
- Key forces creating tertiary structure include covalent bonds, disulfide bridges, hydrogen bonds, hydrophobic interactions, and Van der Waals forces.
Denaturation Effects
- Denaturation disrupts secondary through quaternary structures.
Glycoproteins vs. Proteoglycans
- Glycoproteins: Made mostly of protein; involved in cell signaling.
- Proteoglycans: Rich in carbohydrates; serve as structural components.
Carbohydrate Empirical Formula
- General empirical formula for carbohydrates is CH2O.
Glucose Structure
- Glucose is an aldehyde with four chiral centers, existing as a six-membered ring.
Glucose Storage
- Animals store glucose in glycogen (alpha linkages); plants store it in starch.
Cellulose Structure
- Plant cell walls contain cellulose, characterized by beta linkages.
Hydrolysis Reaction
- Water breaks glycosidic bonds in glycogen, starch, and cellulose, aided by enzymes like amylase.
Four Major Macromolecules
- The primary macromolecules are proteins, lipids, carbohydrates, and nucleic acids.
Nucleotide Composition
- Nucleotides consist of ribose sugar, a nitrogenous base, and a phosphate group.
Nucleic Acid Breakdown
- Nucleic acids are hydrolyzed to nucleotides using water and the aid of nucleases.
Important Nucleotides
- Key nucleotides include FADH, NADH, ATP, and cyclic AMP.
Mineral Functions
- Minerals are inorganic elements essential for:
- Establishing electrochemical gradients
- Acting as cofactors for proteins
- Forming bone matrix compounds.
Enzyme Characteristics
- Enzymes primarily consist of proteins that accelerate reactions by lowering activation energy.
Activation Energy Definition
- The energy required to break reactant bonds and transition into the product state.
Substrate Interaction
- Substrates bind to enzymes at the active site, which is typically larger than the substrate.
Enzyme Models
- Two hypothesized models for enzyme-substrate interaction:
- Lock and Key Model
- Induced Fit Model.
Enzyme Specificity
- Each enzyme is uniquely designed for a specific reaction, enhancing cellular control.
Saturation Kinetics
- Reaction rates increase with substrate availability until enzyme saturation is reached.
Enzyme Regulation Factors
- Enzyme activity is influenced by optimal temperature and pH levels.
Enzyme Regulation Methods
- Cells regulate enzyme function through:
- Inhibition mechanisms
- Production of inactive forms that activate when required.
Types of Enzyme Inhibition
- Inhibition classifications include feedback inhibition and chemical inhibition (e.g., poisons).
Competitive vs. Non-competitive Inhibition
- Competitive inhibition involves competing for the active site, while non-competitive inhibition modifies enzyme shape, reducing substrate affinity.
Irreversible Inhibition
- Irreversible inhibitors covalently bind to the active site, making it permanently inactive.
Respiration Definition
- Respiration encompasses energy-requiring metabolic stages.
Glycolysis Location
- Glycolysis occurs in the cytosol and does not require oxygen.
Glycolysis Products
- Net yield from glycolysis includes 2 ATP, 2 NADH, and 2 pyruvate molecules.
Anaerobic Fate of NADHs
- In the absence of oxygen, NADH is oxidized back to NAD+ via fermentation, yielding CO2 and either ethanol or lactic acid.
Aerobic Fate of Glycolysis Products
- In aerobic conditions, glycolysis products transition into the mitochondria.
Mitochondrial NADH Transport Cost
- Transporting each NADH into the mitochondria requires 1 ATP.
ATP Yield from NADH
- Each NADH generates 3 ATPs during the electron transport chain (ETC).
Pyruvate to Acetyl-CoA Conversion
- Pyruvates are converted to acetyl-CoA in the mitochondrial matrix, feeding into the TCA cycle.
TCA Cycle Products
- Energetic outputs from the TCA cycle include 1 ATP, 3 NADH, and 1 FADH.
Total ATP from Aerobic Respiration
- Aerobic respiration of one glucose molecule yields a total of 36 ATP.
Electron Transport Chain Overview
- The ETC consists of cytochrome proteins in the mitochondrial inner membrane that pass high-energy electrons, creating a proton gradient for ATP synthesis.
Final Electron Acceptor
- Oxygen serves as the final electron acceptor in the ETC.
Fatty Acid Metabolism
- Triglycerides are metabolized into fatty acids and glycerol; glycerol enters glycolysis, while fatty acids convert to acetyl-CoA in the mitochondria.
Protein Metabolism
- Amino acids enter metabolic pathways at varying points, depending on their specific structure.
Gene to Polypeptide Ratio
- Each gene typically results in the production of one polypeptide.
Gene Copies in Prokaryotes
- Prokaryotes generally possess one copy of each gene.
Gene Copies in Eukaryotes
- Eukaryotes generally have one copy of most genes, with some exceptions (e.g., tRNA and rRNA).
Nucleotide Composition Reiterated
- A nucleotide consists of a nitrogenous base, a pentose sugar, and a phosphate group.
Nitrogenous Bases and Nucleosides
- Four nitrogenous bases: Adenine, Thymine, Cytosine, Guanine.
- Four nucleosides: Adenosine, Cytidine, Guanosine
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Test your knowledge of biology with these MCAT practice flashcards. Each card covers key concepts such as hydrolysis and intermolecular bonds, essential for understanding biological processes. Perfect for reviewing before your MCAT exam.