1.1 - Biological Compounds

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    • Monomers are smaller units that can create larger molecules, while polymers are made from lots of monomers bonded together
    • Examples of monomers include glucose, amino acids, and nucleotides
    • Polymers created from monomers include starch, cellulose, glycogen, proteins, DNA, and RNA
    • To create polymers, a condensation reaction is used, involving joining two molecules, creating a chemical bond, and removing water
    • Hydrolysis is the process of breaking apart or splitting the monomers, involving breaking a chemical bond between two molecules using water
    • Carbohydrates are the first biological molecules to study, consisting of monosaccharides, disaccharides, and polysaccharides
    • Monosaccharides include glucose, fructose, and galactose; disaccharides include sucrose, maltose, and lactose; polysaccharides include starch, cellulose, and glycogen
    • Alpha and beta glucose are isomers with different structures, affecting the position of hydrogen and hydroxyl groups on carbon atoms
    • Disaccharides are formed by a condensation reaction creating a glycosidic bond between two monosaccharides
    • Maltose is made from glucose + glucose, lactose from glucose + galactose, and sucrose from glucose + fructose
    • Polysaccharides like starch, cellulose, and glycogen have different structures and functions in plants and animals
    • Starch is a store of glucose, cellulose provides structural strength in plant cell walls, and glycogen is a glucose store in animals
    • Starch and glycogen are made from alpha glucose, while cellulose is made from beta glucose, with different glycosidic bonds
    • Starch has both one to four and one to six glycosidic bonds, while cellulose only has one to four bonds
    • Amylose is unbranched and forms a helix, amylopectin is branched for more enzyme attachment, cellulose forms strong fibrils due to hydrogen bonds
    • Glycogen is highly branched for quick hydrolysis back into glucose, important for animals needing energy
    • Lipids include triglycerides and phospholipids, with triglycerides having three fatty acid chains and a glycerol molecule
    • Triglycerides form through three condensation reactions, losing three water molecules and forming three ester bonds
    • Saturated fatty acids have no double bonds between carbon atoms, while unsaturated fatty acids have at least one double bond
    • Triglycerides function as an energy store due to high energy-storing carbon-hydrogen bonds and metabolic water source, repel water, and have low mass compared to other tissues
    • Lipids have a very low mass compared to other types of tissue in the body, allowing for efficient energy storage without increasing mass as much as extra muscle would
    • Phospholipids have a unique structure with a phosphate group that gives them different properties compared to triglycerides
    • Phospholipids have a hydrophilic head that attracts water and a hydrophobic tail that repels water, allowing them to form a bilayer in water
    • Proteins are polymers made up of amino acid monomers
    • Amino acids have a central carbon with an amine group (NH2), a carboxyl group (COOH), a hydrogen atom, and an R group
    • To form a dipeptide, two amino acids bond together in a condensation reaction, forming a peptide bond
    • The primary structure of a protein is the sequence of amino acids in a polypeptide chain
    • The secondary structure of a protein involves folding or twisting of the primary structure, held in place by hydrogen bonds
    • The tertiary structure of a protein is a unique 3D shape held in place by ionic, hydrogen, and disulfide bonds
    • The quaternary structure of a protein involves multiple polypeptide chains held together by the same bonds as the tertiary structure
    • Enzymes are proteins with a specific active site that catalyze reactions by lowering the activation energy
    • Enzymes have a unique shape in their active site that is complementary to a specific substrate
    • The induced fit model explains how enzymes slightly change shape to bind with substrates and lower the activation energy
    • Factors affecting enzyme-controlled reactions include temperature, pH, substrate concentration, enzyme concentration, and inhibitors
    • Temperature affects enzyme activity by influencing the rate of collisions between enzymes and substrates
    • Substrate concentration affects enzyme activity by determining the rate of collisions between enzymes and substrates
    • pH levels outside the optimum range can denature enzymes by interfering with the charges in the amino acids at the active site
    • Enzyme concentration affects enzyme activity by determining the availability of active sites for substrates
    • Competitive inhibitors bind to the active site of an enzyme, while non-competitive inhibitors bind to the allosteric site, altering the enzyme's shape
    • Biochemical tests for molecules include the iodine test for starch, which turns from orange-brown to blue-black in the presence of starch
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