General Biology: Water, Macromolecules, and Biomolecules
Termini in questo insieme (26)
Water is polar because of the uneven distribution of electrons between oxygen and hydrogen atoms, creating partial positive and negative charges.
Hydrogen bonds between water molecules cause its unique properties like cohesion and high specific heat.
Cohesion: water molecules stick together.
Adhesion: water sticks to other surfaces.
Less dense as a solid: ice floats.
High specific heat: resists temperature change.
Versatile solvent: dissolves many substances.
Hydrophobic substances repel water; hydrophilic substances attract and dissolve in water.
Acids increase H+ concentration; bases decrease H+ concentration by releasing OH- or accepting H+.
pH = \(-\log[H^+]\). The pH scale ranges from 0 (acidic) to 14 (basic), with 7 neutral.
Buffers resist changes in pH by absorbing or releasing H+ ions to maintain stable conditions.
Carbohydrates, lipids, proteins, and nucleic acids.
R group: variable side chain in amino acids.
Functional group: specific group of atoms that give molecules properties.
Monomer: single building block.
Oligomer: few monomers linked.
Polymer: many monomers linked.
Dehydration synthesis joins monomers by removing water.
Hydrolysis breaks polymers by adding water.
Simple sugars, monomers of carbohydrates. Examples: glucose, fructose, galactose.
Long chains of monosaccharides. Examples: starch, glycogen, cellulose, chitin.
Starch: energy storage in plants.
Glycogen: energy storage in animals.
Cellulose: structural support in plant cell walls.
Chitin: structural support in fungi and arthropods.
Triglyceride: lipid made of 3 fatty acids + glycerol.
Fatty acid: long hydrocarbon chain with carboxyl group.
Glycerol: 3-carbon alcohol backbone.
Saturated fats: max # of H atoms, no double bonds, solid at room temp (e.g., butter). Unsaturated fats: one or more double bonds, liquid at room temp (e.g., olive oil).
Phospholipids form the cell membrane bilayer with hydrophilic heads and hydrophobic tails.
Steroids are lipids with a four-ring structure. Examples: cholesterol, testosterone, estrogen.
Amino group (-NH2), carboxyl group (-COOH), hydrogen atom, and R group (side chain).
Covalent bonds that link amino acids together in proteins.
Primary: amino acid sequence.
Secondary: alpha helices and beta sheets.
Tertiary: 3D folding.
Quaternary: multiple polypeptide chains.
Proteins function as enzymes, structural components, storage, transport, movement, hormones, antibodies, and receptors.
Denaturation disrupts protein structure, causing loss of function without breaking peptide bonds.
Sugar (ribose or deoxyribose), phosphate group, and nitrogenous base.
Ribose has a hydroxyl group (-OH) on the 2' carbon; deoxyribose lacks this oxygen (has H instead).
DNA: double-stranded, deoxyribose sugar, stores genetic info.
RNA: single-stranded, ribose sugar, involved in protein synthesis.
Information flows from DNA to RNA to protein.