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Dive into the fundamentals of biochemistry crucial for the AP Biology exam. Learn about elements, atomic structure, bonds, pH, functional groups, carbohydrates, lipids, protein structure, nucleic acids, cells, and transport mechanisms.
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Elements of Life • 25 elements • 96% : C, O, H, N • ~ 4% : P, S, Ca, K & trace elements (ex: Fe, I) Hint: Remember CHNOPS
II. Atomic Structure • Atom = smallest unit of matter that retains properties of an element • Subatomic particles:
Weaker Bonds: Van der Waals Interactions: slight, fleeting attractions between atoms and molecules close together • Weakest bond • Eg. gecko toe hairs + wall surface
1. Polarity of H2O • O- will bond with H+ on a different molecule of H2O = hydrogen bond • H2O can form up to 4 bonds
4. Solvent of life • “like dissolves like”
Acids and Bases Acid: adds H+ (protons); pH<7 Bases: removes protons, adds OH-; pH>7 Buffers = substances which minimize changes in concentration of H+ and OH- in a solution (weak acids and bases) • Buffers keep blood at pH ~7.4 • Good buffer = bicarbonate
ie. amino acid peptide polypeptide protein larger smaller
+ H2O + + H2O +
I. Carbohydrates • Fuel and building • Sugars are the smallest carbs • Provide fuel and carbon • monosaccharide disaccharide polysaccharide • Monosaccharides: simple sugars (ie. glucose) • Polysaccharides: • Storage (plants-starch, animals-glycogen) • Structure (plant-cellulose, arthropod-chitin) • On surface of cell membrane contribute to cell recognition, particularly in the immune response Differ in position & orientation of glycosidic linkage
II. Lipids • Fats: store large amounts of energy • saturated, unsaturated, polyunsaturated • Steroids: cholesterol and hormones • Phospholipids: cell membrane • hydrophilic head, hydrophobic tail • creates bilayer between cell and external environment Hydrophilic head (phospholipid) Hydrophobic tail (Fatty acid tail)
Four Levels of Protein Structure: • Primary • Amino acid sequence • 20 different amino acids • peptide bonds • Secondary • Gains 3-D shape (folds, coils) by H-bonding • α helix, β pleated sheet • Tertiary • Bonding between side chains (R groups) of amino acids • H & ionic bonds, disulfide bridges • Quaternary • 2+ polypeptides bond together
Protein structure and function are sensitive to chemical and physical conditions • Unfolds or denatures if pH and temperature are not optimal
IV. Nucleic Acids Nucleic Acids = Information Monomer: nucleotide
Comparisons of Scopes Light Electron Focuses a beam of electrons through specimen Magnify up to 1,000,000 times Specimen non-living and in vacuum Black and white • Visible light passes through specimen • Light refracts light so specimen is magnified • Magnify up to 1000X • Specimen can be alive/moving • color
Prokaryote Vs. Eukaryote • “before” “kernel” • No nucleus • DNA in a nucleoid • Circular plasmid • Cytosol • No organelles other than ribosomes • Small size • Primitive • Cell membrane/some cell wall • i.e. bacteria • “true” “kernel” • Has nucleus and nuclear membrane • Cytosol • Has organelles with specialized structure and function • Much larger in size • More complex • i.e. plant/animal cell
Cells must remain small to maintain a large surface area to volume ratio • Large S.A. allows increased rates of chemical exchange between cell and environment
Animal cells have intercellular junctions: • Tight junction = prevent leakage • Desomosome = anchor cells together • Gap junction = allow passage of material
Passive vs. Active Transport • Little or no Energy • Moves from high to low concentrations • Moves down the concentration gradient • i.e. diffusion, osmosis, facilitated diffusion (with a transport protein) • Requires Energy (ATP) • Moves from a low concentration to high • Moves against the concentration gradient • i.e. pumps, exo/endocytosis
Exocytosis and Endocytosis transport large molecules 3 Types of Endocytosis: • Phagocytosis (“cell eating” - solids) • Pinocytosis (“cell drinking” - fluids) • Receptor-mediated endocytosis • Very specific • Substances bind to receptors on cell surface