BackGeneral Biology: Macromolecules, Cell Structure, Membranes, and Metabolism
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Chapter 5: Biological Macromolecules
Monomer vs Polymer
Biological macromolecules are large molecules composed of smaller subunits called monomers. When monomers join together, they form polymers through specific chemical reactions.
Monomer: A small molecule that can bind to other similar molecules to form a polymer.
Polymer: A large molecule made up of repeating monomer units.
Examples: Monosaccharides (monomers) form polysaccharides (polymers); amino acids (monomers) form proteins (polymers).
Synthesis and Breakdown of Polymers
Dehydration: A chemical reaction that joins monomers by removing a water molecule.
Hydrolysis: A reaction that breaks polymers into monomers by adding water.
Equation:
Carbohydrates
Carbohydrates are organic molecules consisting of carbon, hydrogen, and oxygen, typically in a 1:2:1 ratio. They serve as energy sources and structural components.
Structure and Function: Provide energy (glucose), store energy (starch, glycogen), and provide structural support (cellulose, chitin).
Linkage: Glycosidic bonds connect monosaccharides.
Monosaccharide vs Disaccharide vs Oligosaccharide vs Polysaccharide:
Monosaccharide: Single sugar unit (e.g., glucose, fructose).
Disaccharide: Two monosaccharides joined (e.g., sucrose = glucose + fructose).
Oligosaccharide: 3-10 monosaccharide units.
Polysaccharide: Many monosaccharides (e.g., starch, glycogen, cellulose).
Storage Polysaccharides: Starch (plants), glycogen (animals).
Structural Polysaccharides: Cellulose (plants), chitin (arthropods, fungi).
Lipids
Lipids are hydrophobic molecules, including fats, phospholipids, and steroids, important for energy storage, membrane structure, and signaling.
Fats (Triglycerides):
Structure: Glycerol + 3 fatty acids.
Function: Long-term energy storage, insulation, protection.
Linkage: Ester bonds.
Saturated vs Unsaturated Fatty Acids: Saturated (no double bonds, solid at room temp), Unsaturated (one or more double bonds, liquid at room temp).
Phospholipids:
Structure: Glycerol, 2 fatty acids, phosphate group.
Function: Main component of cell membranes; form bilayers.
Behavior in Bilayer: Hydrophilic heads face water, hydrophobic tails face inward.
Steroids:
Structure: Four fused carbon rings.
Examples: Cholesterol, steroid hormones (e.g., signaling hormones).
Proteins
Proteins are polymers of amino acids that perform a wide range of functions, including catalysis, structure, transport, and signaling.
Structure and Function: Determined by amino acid sequence and folding.
Linkage: Peptide bonds between amino acids.
Monomer vs Polymer: Amino acids (monomers) form polypeptides/proteins (polymers).
Structure of Amino Acid: Central carbon, amino group, carboxyl group, hydrogen, R group (side chain).
20 Amino Acids:
Categories: Non-polar, polar, acidic, basic, aromatic.
Naming: 3-letter and 1-letter abbreviations.
Classification: Know which amino acids fall into each category.
Nucleic Acids
Nucleic acids (DNA and RNA) store and transmit genetic information.
Structure and Function: Polymers of nucleotides; DNA stores genetic information, RNA transmits and translates it.
Linkage: Phosphodiester bonds between nucleotides.
DNA vs RNA:
Nucleotide vs Nucleoside: Nucleotide = base + sugar + phosphate; Nucleoside = base + sugar.
Bases: Purines (A, G) vs Pyrimidines (C, T, U).
Sugars: Deoxyribose (DNA) vs Ribose (RNA).
Double vs Single Stranded: DNA is usually double-stranded; RNA is usually single-stranded.
Complementary Base Pairing: A-T (DNA), A-U (RNA), G-C.
Gene Expression: DNA → RNA → Protein (Central Dogma).
Chapter 6: Cell Structure
Cell Theory
All living organisms are composed of cells, which are the basic units of life.
Eukaryotic vs Prokaryotic: Eukaryotes have a nucleus and membrane-bound organelles; prokaryotes do not.
The Nucleus
Structure: Nuclear envelope, nucleolus, chromatin.
Function: Stores genetic material, site of RNA synthesis.
Ribosomes
Structure: Composed of rRNA and proteins.
Function: Protein synthesis.
The Endomembrane System
Nuclear Envelope: Double membrane surrounding the nucleus.
Endoplasmic Reticulum (ER): Rough (with ribosomes, protein synthesis) and smooth (lipid synthesis, detoxification).
Golgi Apparatus: Modifies, sorts, and packages proteins and lipids.
Lysosomes: Contain digestive enzymes for breakdown of macromolecules.
Vacuoles: Storage and structural support (especially in plants).
Mitochondria, Chloroplasts, Peroxisomes
Mitochondria: Site of cellular respiration and ATP production.
Chloroplasts: Site of photosynthesis in plants and algae.
Peroxisomes: Break down fatty acids and detoxify harmful substances.
The Cytoskeleton
The cytoskeleton provides structural support, cell shape, and facilitates movement.
Components: Microtubules, microfilaments, intermediate filaments.
Microtubules: Hollow tubes; involved in cell division, organelle movement, cilia, and flagella.
Microfilaments: Actin filaments; involved in muscle contraction, cell movement.
Intermediate Filaments: Provide mechanical support.
Extracellular Components
Cell Wall: Provides structure and protection (plants, fungi, some protists).
Extracellular Matrix (ECM): Network of proteins and carbohydrates outside animal cells; provides support and signaling.
Cell Junctions: Plasmodesmata (plants), tight junctions, desmosomes, gap junctions (animals).
Chapter 7: Membranes and Transport
Passive vs Active vs Bulk Transport
Passive Transport: Movement of substances down their concentration gradient without energy input (e.g., diffusion, osmosis).
Active Transport: Movement against the concentration gradient, requires energy (e.g., Na+/K+ pump).
Bulk Transport: Movement of large particles via vesicles (e.g., endocytosis, exocytosis).
Plasma Membrane
Phospholipid Amphipathic Structure: Hydrophilic heads, hydrophobic tails.
Fluid Mosaic Model: Membrane is a fluid structure with proteins embedded in or attached to a bilayer of phospholipids.
Fluidity of Membranes: Affected by temperature, fatty acid composition, cholesterol.
Selective Permeability
Solute vs Solvent: Solute is dissolved, solvent does the dissolving.
Components that Cross Easily: Small, nonpolar molecules cross easily; large or charged molecules do not.
Membrane Proteins
Peripheral vs Integral Proteins: Peripheral are on the surface; integral span the membrane.
Types: Transport, transmembrane (carrier and channel), receptor, enzymatic, structural.
Transport Processes
Diffusion: Movement of molecules from high to low concentration.
Osmosis: Diffusion of water across a selectively permeable membrane.
Facilitated Diffusion: Passive transport via proteins.
Tonicity: Effect of solute concentration on cell volume (hypotonic, hypertonic, isotonic).
Active Transport and Cotransport
Active Transport: Requires energy (ATP), moves substances against gradient (e.g., Na+/K+ pump).
Cotransport: Coupled transport of two substances (e.g., sodium/glucose cotransport).
Bulk Transport
Exocytosis: Vesicles fuse with membrane to release contents outside cell.
Endocytosis: Cell takes in materials via vesicles (phagocytosis, pinocytosis, receptor-mediated endocytosis).
Chapter 8: Metabolism and Enzymes
Metabolic Pathways
Catabolic Pathways: Break down molecules, release energy.
Anabolic Pathways: Build complex molecules, consume energy.
Forms of Energy
Kinetic Energy: Energy of motion.
Potential Energy: Stored energy.
Chemical Energy: Potential energy in chemical bonds.
Laws of Thermodynamics
First Law: Energy cannot be created or destroyed, only transformed.
Second Law: Every energy transfer increases the entropy (disorder) of the universe.
ATP and Cellular Work
ATP: Adenosine triphosphate, main energy currency of the cell.
Energy Coupling: Use of exergonic processes to drive endergonic ones.
ATP Regeneration: ATP is regenerated from ADP and phosphate.
Equation:
Enzymes
Structure and Function: Biological catalysts that speed up chemical reactions by lowering activation energy.
Energy of Activation: Minimum energy required to start a reaction.
Substrate Specificity: Enzymes bind specific substrates at the active site (induced fit model).
Enzyme Kinetics: Rate of reaction affected by substrate concentration, temperature, pH.
Cofactors: Non-protein helpers (metal ions, vitamins).
Regulation:
Allosteric Regulation: Enzyme activity regulated by binding of molecules at sites other than the active site (activation or inhibition).
Feedback Inhibition: End product of a pathway inhibits an earlier step.
Compartmentalization: Enzymes are often localized within specific cellular compartments for efficiency.