Fiche de révision : Fundamentals of Biological Chemistry

📋 Course Outline

  1. Nutrients and Classification
  2. Biochemistry Fundamentals
  3. Water Properties and Behavior
  4. Ionization and pH
  5. Organic Chemistry Structures
  6. Carbohydrate Structure and Function
  7. Protein Structure and Function
  8. Lipid Types and Functions
  9. Macromolecule Bonds
  10. Cell Membrane Structure
  11. Transport Mechanisms
  12. Enzyme Catalysis and Inhibition

📖 1. Nutrients and Classification

🔑 Key Concepts & Definitions

  • Nutrient: A substance required by an organism to maintain life, growth, and health. Includes macronutrients and micronutrients.
  • Macronutrient: Nutrients needed in large amounts for energy and growth; includes carbohydrates, proteins, and fats.
  • Micronutrient: Nutrients required in small amounts for proper physiological functions; includes vitamins and minerals.
  • Carbohydrates: Organic molecules primarily used as a source of energy; composed of carbon, hydrogen, and oxygen (e.g., bread, grains).
  • Proteins: Large biomolecules made of amino acids; essential for building tissues, enzymes, and hormones.
  • Vitamins: Organic compounds needed in small quantities for metabolic processes; e.g., Vitamin A, B12, E, K.

📝 Essential Points

  • Nutrients are classified based on the amount required: macronutrients (large amounts) and micronutrients (small amounts).
  • Carbohydrates and proteins are primary energy sources; fats provide long-term energy storage.
  • Minerals (e.g., calcium, iron) are inorganic micronutrients vital for functions like bone health and oxygen transport.
  • Vitamins facilitate enzyme functions and metabolic pathways; deficiencies can cause health issues.
  • Water is also a vital nutrient, essential for biochemical reactions, temperature regulation, and transport.

💡 Key Takeaway

Nutrients are essential substances classified into macronutrients and micronutrients, each playing specific roles in maintaining health, growth, and metabolic functions. Proper intake of all nutrient types is crucial for optimal organism functioning.

📖 2. Biochemistry Fundamentals

🔑 Key Concepts & Definitions

  • Nutrient: A substance required by organisms for growth, energy, and maintenance. Includes macronutrients (carbohydrates, fats, proteins) and micronutrients (vitamins, minerals).

  • Macronutrient: Nutrients needed in large amounts; primarily carbohydrates, fats/lipids, and proteins.

  • Micronutrient: Nutrients needed in small amounts; includes vitamins and minerals.

  • Covalent Bond: A chemical bond where two atoms share one or more pairs of electrons, forming molecules.

  • Electronegativity (EN): An atom’s tendency to attract shared electrons in a bond. Determines bond polarity: nonpolar, polar covalent, or ionic.

  • Water Properties: Water is a polar molecule capable of hydrogen bonding, leading to high melting/boiling points, cohesion, adhesion, and unique solid-state density.

📝 Essential Points

  • Water's Role: Acts as a universal solvent, facilitates biochemical reactions, and forms hydration shells around ions and polar molecules.

  • pH and Ionization: Water autoionizes into H₃O⁺ and OH⁻; acids increase H⁺ concentration, bases increase OH⁻. pH measures H⁺ concentration; neutral pH is 7.

  • Organic Chemistry: Carbon’s ability to form cyclic and chain structures underpins biological molecules. Functional groups (e.g., hydroxyl, carbonyl, amino, carboxyl) determine molecule properties and reactivity.

  • Carbohydrates: Composed of monosaccharides linked by glycosidic bonds; serve as energy sources and structural components. Polysaccharides include starch, glycogen, and cellulose.

  • Proteins: Made of amino acids linked by peptide bonds; their structure (primary to quaternary) determines function in enzymes, hormones, and structural components.

  • Lipids: Include fatty acids, fats, phospholipids, steroids, and waxes; primarily serve energy storage, membrane formation, and signaling.

  • Cell Membrane: Composed of a phospholipid bilayer with embedded proteins; exhibits fluid mosaic behavior and selective permeability.

  • Enzymes: Biological catalysts that lower activation energy, speeding up reactions. Function via models like lock-and-key and induced fit; activity can be regulated by inhibitors and cofactors.

💡 Key Takeaway

Biochemistry explains how molecules like water, carbohydrates, proteins, and lipids interact and function within living organisms, underpinning all biological processes through chemical structures and reactions.

📖 3. Water Properties and Behavior

🔑 Key Concepts & Definitions

  • Polarity: Water is a polar molecule, meaning it has a partial positive charge on hydrogen atoms and a partial negative charge on oxygen, enabling hydrogen bonding.
  • Hydrogen Bond: A weak attraction between a hydrogen atom covalently bonded to an electronegative atom (like oxygen) and another electronegative atom. Responsible for water’s high boiling point and surface tension.
  • Cohesion: The attraction between water molecules due to hydrogen bonding, leading to surface tension and water’s ability to form droplets.
  • Adhesion: The attraction between water molecules and other substances, aiding in capillary action.
  • Density Anomaly of Water: Water expands upon freezing, making ice less dense than liquid water, which allows ice to float.
  • pH and Ionization: Water autoionizes into H₃O⁺ (hydronium) and OH⁻ (hydroxide), with a neutral pH of 7, indicating equal H⁺ and OH⁻ concentrations.

📝 Essential Points

  • Water's strong intermolecular forces (hydrogen bonds) give it unique properties such as high surface tension, high specific heat, and solvent abilities.
  • Freezing causes water molecules to form a crystalline lattice, decreasing density and causing ice to float.
  • Water's solvent properties: It surrounds ions and polar molecules, forming hydration shells, which facilitate dissolving salts and other polar substances.
  • Autoionization of water is reversible and maintains a neutral pH of 7 at 25°C.
  • pH scale: Measures H⁺ concentration; acids have pH < 7, bases > 7, and pure water is neutral at pH 7.

💡 Key Takeaway

Water’s polarity and hydrogen bonding give it unique physical and chemical properties essential for life, including its role as a universal solvent, its high specific heat, and its behavior during freezing and melting.

📖 4. Ionization and pH

🔑 Key Concepts & Definitions

  • Autoionization of Water: The reversible process where two water molecules transfer a proton, forming hydronium (H₃O⁺) and hydroxide (OH⁻) ions: H2OH++OH\mathrm{H_2O} \leftrightarrow \mathrm{H^+} + \mathrm{OH^-}

  • pH: A logarithmic scale measuring the concentration of hydrogen ions (H⁺) in a solution: pH=log[H+]\mathrm{pH} = -\log[\mathrm{H^+}] Ranges from 0 (acidic) to 14 (basic), with 7 being neutral.

  • Acids: Substances that increase H⁺ concentration in solution; typically have ionizable hydrogen atoms (e.g., HBr, HCl).

  • Bases: Substances that increase OH⁻ concentration; can contain ionizable hydroxide groups or remove H⁺ from water (e.g., NaOH, NH₃).

  • Ionization of Acids and Bases: Process where acids release H⁺ ions and bases release OH⁻ ions in solution, affecting pH.

📝 Essential Points

  • Water's autoionization constant (KwK_w) at 25°C is 1.0×10141.0 \times 10^{-14}, meaning: [H+][OH]=1.0×1014[\mathrm{H^+}][\mathrm{OH^-}] = 1.0 \times 10^{-14}
  • Neutral solutions have equal H⁺ and OH⁻ concentrations (10710^{-7} M each), corresponding to pH 7.
  • Acidic solutions have [H+]>107[\mathrm{H^+}] > 10^{-7} M, pH < 7.
  • Basic solutions have [H+]<107[\mathrm{H^+}] < 10^{-7} M, pH > 7.
  • The pH scale is logarithmic; a one-unit change in pH corresponds to a tenfold change in H⁺ concentration.
  • Buffer systems maintain pH stability by neutralizing added acids or bases (e.g., carbonic acid-bicarbonate buffer).

💡 Key Takeaway

The pH of a solution reflects its H⁺ concentration, directly influencing biochemical reactions and cellular functions; understanding ionization processes helps explain how acids, bases, and buffers regulate biological systems.

📖 5. Organic Chemistry Structures

🔑 Key Concepts & Definitions

  • Carbon Skeleton: The chain or ring structure formed by carbon atoms in an organic molecule, serving as the backbone for functional groups and overall molecular shape.

  • Functional Group: A specific group of atoms within a molecule that determines its chemical reactivity and properties (e.g., hydroxyl, carbonyl, amino, carboxyl).

  • Hydrocarbon: An organic compound consisting entirely of carbon and hydrogen atoms, classified into alkanes (single bonds), alkenes (double bonds), and alkynes (triple bonds).

  • Isomer: Molecules with the same molecular formula but different arrangements of atoms, resulting in different structures and properties (e.g., structural isomers, stereoisomers).

  • Aromatic Ring: A cyclic, planar structure with alternating double bonds, such as benzene, exhibiting resonance stability.

  • Glycosidic Bond: A covalent bond formed between two monosaccharides during carbohydrate polymerization, linking their anomeric carbon atoms.

📝 Essential Points

  • Carbon's ability to form four covalent bonds allows for diverse structures, including chains, rings, and complex branched molecules.

  • Functional groups are key to the chemical behavior of organic molecules; their polarity influences solubility and reactivity.

  • Structural isomers differ in the connectivity of their atoms, while stereoisomers differ in spatial arrangement; both impact biological activity.

  • Cyclic structures like alicyclic and aromatic rings are common in organic compounds, with aromatic rings providing stability due to resonance.

  • The type of hydrocarbon (alkane, alkene, alkyne) affects the molecule's reactivity and physical properties like boiling point and solubility.

  • Glycosidic bonds link monosaccharides into disaccharides and polysaccharides, affecting digestibility and biological function.

💡 Key Takeaway

Organic molecules are primarily built around carbon skeletons with various functional groups, enabling a vast diversity of structures and chemical behaviors essential for life processes.

📖 6. Carbohydrate Structure and Function

🔑 Key Concepts & Definitions

  • Monosaccharide: The simplest carbohydrate, a single sugar molecule with the general formula CnH2nOn (e.g., glucose, fructose).
  • Glycosidic Bond: A covalent bond formed between two monosaccharides during the formation of disaccharides and polysaccharides.
  • Anomer: Isomers of cyclic monosaccharides that differ in the configuration around the anomeric carbon (α or β).
  • Polysaccharide: Large carbohydrate molecules composed of many monosaccharide units linked by glycosidic bonds (e.g., starch, glycogen, cellulose).
  • Alpha (α) and Beta (β) Glucose: Isomers of glucose differing in the orientation of the hydroxyl group on the anomeric carbon, influencing digestibility and function.
  • Hydrolysis: The chemical breakdown of a compound due to reaction with water, used to break down polysaccharides into monosaccharides.

📝 Essential Points

  • Carbohydrates are primarily energy sources, with the general formula Cx(H2O)x, reflecting their water content.
  • Monosaccharides can exist in linear or cyclic forms; cyclic forms are more common in biological systems.
  • The configuration of the hydroxyl group on the anomeric carbon (C1) determines whether the sugar is α or β, affecting properties like digestibility (e.g., humans digest α-glucose in starch but not β-glucose in cellulose).
  • Disaccharides (e.g., sucrose, lactose, maltose) are formed via glycosidic bonds and are broken down into monosaccharides during digestion.
  • Polysaccharides serve various functions: energy storage (glycogen in animals, starch in plants) and structural support (cellulose in plant cell walls).
  • The digestibility of polysaccharides depends on the type of glycosidic linkage; humans can digest α-linkages but not β-linkages like those in cellulose.

💡 Key Takeaway

Carbohydrates are vital biological molecules that vary from simple sugars to complex polysaccharides, with their structure—especially the type of glycosidic bonds and configuration—dictating their biological roles and digestibility.

📖 7. Protein Structure and Function

🔑 Key Concepts & Definitions

  • Amino Acid: Organic molecules with an amino group (-NH₂) and a carboxyl group (-COOH); the building blocks of proteins.
  • Primary Structure: The linear sequence of amino acids in a polypeptide chain.
  • Secondary Structure: Local folding patterns of the polypeptide backbone, mainly alpha-helices and beta-sheets stabilized by hydrogen bonds.
  • Tertiary Structure: The overall 3D shape of a single polypeptide, formed by interactions between R-groups, including hydrogen bonds, ionic bonds, disulfide bridges, and hydrophobic interactions.
  • Quaternary Structure: The arrangement and interaction of multiple polypeptide chains (subunits) in a protein.
  • Denaturation: The process where a protein loses its native structure due to heat, pH changes, or chemicals, often resulting in loss of function.

📝 Essential Points

  • Proteins are composed of amino acids linked by peptide bonds, forming polypeptides.
  • The structure of a protein determines its function; even small changes can alter activity.
  • Hydrogen bonds, ionic interactions, sulfur bridges, and van der Waals forces stabilize protein structures.
  • Proteins can be denatured by heat or chemicals, disrupting secondary and tertiary structures but often leaving primary structure intact.
  • Enzymes are proteins that catalyze biochemical reactions by lowering activation energy, often exhibiting specificity for their substrates.
  • Protein functions include hormone signaling, enzyme activity, structural support, transport (e.g., hemoglobin), immune response, and cell signaling.

💡 Key Takeaway

Protein structure is hierarchical, with each level—from primary to quaternary—playing a crucial role in determining the protein's function; understanding these structures helps explain how proteins perform their diverse biological roles.

📖 8. Lipid Types and Functions

🔑 Key Concepts & Definitions

  • Lipids: Organic molecules characterized by their insolubility in water, primarily composed of hydrocarbons, serving roles in energy storage, membrane structure, and signaling.

  • Fatty Acids: Hydrocarbon chains with a terminal carboxyl group (-COOH); can be saturated (single bonds) or unsaturated (double/triple bonds).

  • Saturated Fatty Acids: Fatty acids with only single bonds between carbons, resulting in straight chains that pack tightly, usually solid at room temperature.

  • Unsaturated Fatty Acids: Fatty acids containing one or more double or triple bonds, causing bends in the chain; often liquid at room temperature.

  • Phospholipids: Lipids with two fatty acids, a glycerol backbone, and a phosphate group; major components of cell membranes forming a bilayer.

  • Steroids: Lipids with four fused rings, such as cholesterol; function in membrane fluidity and as precursors to hormones like testosterone and estrogen.

📝 Essential Points

  • Lipids are vital for long-term energy storage (fats), insulation (adipose tissue), membrane formation (phospholipids), and cell signaling (steroids).

  • Fats are formed via dehydration synthesis, linking glycerol to up to three fatty acids through ester bonds.

  • Saturated fats tend to be solid at room temperature, while unsaturated fats (especially cis forms) are liquid, affecting their biological roles and health implications.

  • Trans fats are artificially produced unsaturated fats with linear chains, associated with health risks.

  • Phospholipids form bilayers due to their polar phosphate head and nonpolar fatty acid tails, creating semi-permeable membranes.

  • Steroids like cholesterol modulate membrane fluidity and serve as hormone precursors.

💡 Key Takeaway

Lipids are diverse molecules essential for energy storage, membrane structure, and signaling, with their physical and chemical properties influencing their biological functions and health impacts.

📖 9. Macromolecule Bonds

🔑 Key Concepts & Definitions

  • Glycosidic (Ether) Bond: A covalent bond formed between two monosaccharides through a dehydration reaction, linking the carbohydrate units in polysaccharides like starch and glycogen.

  • Peptide (Amide) Bond: A covalent bond that connects amino acids in proteins, formed via a dehydration synthesis between the amino group of one amino acid and the carboxyl group of another.

  • Ester Bond: A covalent linkage formed between a fatty acid and glycerol in lipids, created through dehydration synthesis between the hydroxyl group of glycerol and the carboxyl group of a fatty acid.

  • Hydrogen Bond: A weak attraction between a hydrogen atom covalently bonded to an electronegative atom (like oxygen or nitrogen) and another electronegative atom, crucial for stabilizing protein secondary structures and DNA double helix.

  • Disulfide Bridge: A covalent bond between two sulfur atoms of cysteine amino acids, providing stability to protein tertiary and quaternary structures.

📝 Essential Points

  • Macromolecules are held together by specific covalent bonds: glycosidic in carbohydrates, peptide in proteins, and ester in lipids.

  • Hydrogen bonds, although weak individually, collectively stabilize the three-dimensional structures of proteins and nucleic acids.

  • Disulfide bridges are important for the stability and proper folding of many extracellular proteins.

  • The type of bond influences the molecule's structure, function, and digestibility (e.g., body cannot digest b-glucose polymers due to glycosidic linkage differences).

  • Bond formation involves dehydration synthesis, releasing water, while breaking bonds (hydrolysis) requires water.

💡 Key Takeaway

Understanding the specific covalent and hydrogen bonds that link macromolecules is essential for grasping their structure-function relationships and how they are processed in biological systems.

📖 10. Cell Membrane Structure

🔑 Key Concepts & Definitions

  • Phospholipid Bilayer: A double layer of phospholipids forming the fundamental structure of the cell membrane, with hydrophilic heads facing outward and hydrophobic tails inward, creating a semi-permeable barrier.

  • Fluid Mosaic Model: Describes the cell membrane as a dynamic, flexible structure composed of phospholipids, proteins, cholesterol, and carbohydrates, where components can move laterally within the layer.

  • Membrane Proteins: Embedded or attached proteins that serve various functions such as transport, signal transduction, and structural support; classified as integral (transmembrane) or peripheral.

  • Selective Permeability: The property of the cell membrane allowing certain molecules to pass through while blocking others, thus maintaining homeostasis.

  • Transport Proteins: Specialized proteins facilitating the movement of substances across the membrane, including channel proteins, carrier proteins, and pumps.

  • Cholesterol: Lipid molecules interspersed within the phospholipid bilayer that modulate membrane fluidity and stability.

📝 Essential Points

  • The phospholipid bilayer forms the basic structure, providing a flexible yet protective barrier that is selectively permeable.

  • Proteins embedded in the membrane perform critical functions such as transporting ions and molecules, receiving signals, and maintaining cell shape.

  • The fluid mosaic model emphasizes the lateral movement of membrane components, essential for membrane function and cell signaling.

  • Cholesterol maintains membrane fluidity, preventing the bilayer from becoming too rigid or too fluid, especially in varying temperature conditions.

  • Transport mechanisms include passive processes like diffusion and osmosis, and active processes requiring energy (ATP), such as active transport and endocytosis.

  • The cell membrane's structure is crucial for maintaining homeostasis, communication, and interaction with the environment.

💡 Key Takeaway

The cell membrane's fluid mosaic structure, composed of phospholipids, proteins, and cholesterol, enables it to be selectively permeable, flexible, and functional in maintaining cellular integrity and communication.

📖 11. Transport Mechanisms

🔑 Key Concepts & Definitions

  • Diffusion: The passive movement of molecules from an area of high concentration to an area of low concentration across a semi-permeable membrane until equilibrium is reached.

  • Osmosis: A specific type of diffusion involving the movement of water molecules through a semi-permeable membrane from a region of lower solute concentration to higher solute concentration.

  • Active Transport: The movement of molecules against their concentration gradient, from low to high concentration, requiring energy in the form of ATP.

  • Facilitated Diffusion: Passive transport of molecules across a membrane via specific carrier proteins or channels, without energy expenditure, down their concentration gradient.

  • Endocytosis: Active process where the cell engulfs large molecules or particles by wrapping the membrane around them, forming vesicles inside the cell.

  • Exocytosis: The process by which cells expel large molecules or waste by enclosing them in vesicles that fuse with the cell membrane, releasing contents outside.

📝 Essential Points

  • Passive vs. Active Transport: Passive processes (diffusion, osmosis, facilitated diffusion) do not require energy and rely on concentration gradients. Active processes (active transport, endocytosis, exocytosis) require energy to move substances against their gradients.

  • Membrane Permeability: The cell membrane's selective permeability allows certain molecules to pass freely (like small nonpolar molecules) while restricting others (like ions or large molecules).

  • Osmotic Effects: Changes in water movement can cause cells to swell (lysis in hypotonic solutions) or shrink (plasmolysis in hypertonic solutions), affecting cell function.

  • Transport Proteins: Specific channels and carriers facilitate facilitated diffusion and active transport, ensuring selective and efficient movement of molecules.

  • Energy Use: Active transport mechanisms like the sodium-potassium pump maintain essential concentration gradients for cell function.

💡 Key Takeaway

Transport mechanisms enable cells to regulate their internal environment by controlling the movement of substances through the membrane, balancing passive and active processes to sustain life functions.

📖 12. Enzyme Catalysis and Inhibition

🔑 Key Concepts & Definitions

  • Enzyme: A biological catalyst, usually a protein, that speeds up chemical reactions by lowering activation energy without being consumed in the process.
  • Active Site: The specific region on an enzyme where substrate molecules bind and undergo a chemical reaction.
  • Catalyst: A substance that increases the rate of a chemical reaction by reducing the activation energy barrier.
  • Inhibition: The process of decreasing enzyme activity, which can be reversible or irreversible.
  • Competitive Inhibition: When an inhibitor binds to the active site of an enzyme, blocking substrate binding.
  • Allosteric Site: A separate site on an enzyme where regulatory molecules bind, causing conformational changes that affect enzyme activity.

📝 Essential Points

  • Enzymes function by forming an enzyme-substrate complex, facilitating the conversion of substrates into products.
  • The Lock and Key model suggests enzymes are specific to their substrates, fitting together precisely. The Induced Fit model states enzymes change shape upon substrate binding for a tighter fit.
  • Enzyme activity can be regulated via allosteric regulation, where molecules bind to allosteric sites, activating or inhibiting the enzyme.
  • Inhibitors can be reversible (competitive, allosteric) or irreversible (permanent binding, denaturation).
  • Cofactors (metal ions) and coenzymes (organic molecules like vitamins) are essential for enzyme activity.
  • Enzyme reactions are sensitive to environmental factors such as temperature, pH, and substrate concentration.

💡 Key Takeaway

Enzymes are highly specific biological catalysts that regulate biochemical reactions through mechanisms like substrate binding and inhibition, with their activity finely tuned by structural and environmental factors.

📊 Synthesis Tables

Feature / ConceptWater Properties & BehaviorIonization & pH
PolarityWater is polar, enabling hydrogen bondingpH measures H⁺ concentration in solution
Hydrogen BondingResponsible for high boiling point, cohesionInfluences autoionization equilibrium
Cohesion & AdhesionWater molecules attract each other & other surfacesAffects transport in biological systems
Density of IceIce floats because solid water is less denseNot directly related to pH but affects environment
Solvent PropertiesDissolves polar substances, salts, sugarspH affected by dissolved acids/bases
Autoionization of WaterProduces H₃O⁺ and OH⁻ ionsDetermines neutral pH (7) at 25°C
Feature / ConceptOrganic Chemistry StructuresCarbohydrate & Protein Structure & Function
Carbon SkeletonChains and rings of carbon, backbone of organicsMonosaccharides, amino acids, fatty acids
Functional GroupsHydroxyl, carbonyl, amino, carboxyl groupsDetermine reactivity and properties
Monomers & PolymersMonosaccharides, amino acids, fatty acidsPolysaccharides, proteins, lipids
Bond TypesCovalent bonds (glycosidic, peptide, ester)Peptide bonds, glycosidic bonds, ester bonds
Structural HierarchyPrimary to quaternary structures in proteinsPrimary (sequence), secondary (helix), tertiary, quaternary

⚠️ Common Pitfalls & Confusions

  1. Confusing Water Polarity with Nonpolar Molecules: Water is polar; nonpolar molecules (like oils) do not dissolve well.
  2. Misinterpreting pH Scale: pH is logarithmic; a change of 1 unit equals tenfold H⁺ difference.
  3. Assuming All Organic Molecules Are Hydrophobic: Many, like carbohydrates and amino acids, are polar and soluble.
  4. Mixing Up Covalent and Ionic Bonds: Covalent bonds involve shared electrons; ionic bonds involve transfer of electrons.
  5. Overlooking Functional Group Influence: Functional groups determine molecule reactivity, not just backbone structure.
  6. Misidentifying Monomers and Polymers: Monosaccharides are building blocks of polysaccharides; amino acids form proteins.
  7. Confusing Enzyme Inhibition Types: Competitive vs non-competitive inhibitors differ in binding site and effect.
  8. Assuming All Lipids Are Hydrophobic: Some lipids, like phospholipids, have polar head groups.
  9. Misunderstanding Cell Membrane Fluidity: It depends on fatty acid saturation and cholesterol content.
  10. Incorrectly Linking Structure to Function: Protein shape (structure) directly affects its function.

✅ Exam Checklist

  • Recall the classification of nutrients into macronutrients and micronutrients.
  • Describe water’s unique physical and chemical properties resulting from hydrogen bonding.
  • Explain water autoionization and how it relates to pH.
  • Define pH, acids, bases, and buffers; understand their biological significance.
  • Identify key functional groups in organic molecules and their roles.
  • Distinguish between monosaccharides, disaccharides, and polysaccharides.
  • Describe protein structure levels and how they determine function.
  • List lipid types and their biological roles.
  • Understand covalent bonds in macromolecules and their significance.
  • Describe the structure of the cell membrane and its fluid mosaic model.
  • Explain transport mechanisms: passive (diffusion, facilitated diffusion) and active transport.
  • Outline enzyme catalysis, including the lock-and-key and induced fit models.
  • Recognize different enzyme inhibitors and their effects on enzyme activity.

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1. What does nutrient classification refer to?

2. What is the value of the autoionization constant ($K_w$) of water at 25°C?

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Mémorisez les concepts clés de Fundamentals of Biological Chemistry avec 24 flashcards interactives.

Lipid — main function?

Energy storage and membrane formation.

Carbohydrate — monomer?

Monosaccharide.

Water — essential role?

Biochemical reactions and temperature regulation.

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