What are the major types of intermolecular forces, their relative strengths, and the types of molecules involved in each, and how do they relate to biological macromolecules, lipids, nucleotides, and other biomolecules?

Intermolecular forces include hydrogen bonding (strongest, between molecules with H bonded to N, O, or F), dipole-dipole interactions (between polar molecules), and London dispersion forces (weakest, between all molecules due to temporary dipoles). Ion-dipole forces occur between ions and polar molecules. Polymers are large molecules made of repeating subunits called monomers, connected through condensation reactions (forming covalent bonds with water release) or addition reactions (no byproducts). Major biological macromolecules include proteins (amino acid monomers), nucleic acids (nucleotide monomers), carbohydrates (monosaccharide monomers), and lipids (fatty acids and glycerol). "Monomer types are conserved" means the same types of monomers are used across all organisms. Lipids include triglycerides (energy storage), phospholipids (membrane components), steroids (signaling molecules), and sphingolipids (membrane components). Nucleotides include ATP, GTP, CTP, and UTP, which store energy in phosphoanhydride bonds and release it through hydrolysis. Polynucleotides are formed when nucleotides connect through phosphodiester bonds between the 3' hydroxyl and 5' phosphate groups. Amino acids contain an amino group, carboxyl group, and R-group (side chain) attached to a central carbon. They form peptide bonds through dehydration synthesis between the amino group of one amino acid and the carboxyl group of another. The acid dissociation constant (Ka) represents the strength of an acid, with pH = pKa + log([A-]/[HA]). Buffers work best when pH is within ±1 of the buffer's pKa. Protein structure includes primary (amino acid sequence), secondary (alpha helices, beta sheets stabilized by hydrogen bonds), tertiary (overall 3D structure stabilized by various interactions), and quaternary (multiple polypeptide chains). In polypeptides, rotation occurs around single bonds but not peptide bonds due to resonance. Enzymes are biological catalysts that lower activation energy without changing reaction equilibrium. They work through mechanisms including proximity effects, acid-base catalysis, covalent catalysis, and strain. Enzyme kinetics are described by parameters like Vmax (maximum reaction rate) and Km (substrate concentration at half Vmax). Allosteric enzymes can be regulated by activators or inhibitors binding at sites other than the active site. Carbohydrates exist in linear and cyclic forms, with the anomeric carbon determining alpha or beta configuration. Glycosidic bonds connect monosaccharides to form disaccharides and polysaccharides. Biological membranes consist of amphiphilic phospholipid bilayers with embedded proteins that facilitate transport through passive diffusion, facilitated diffusion, or active transport. Cell signaling involves signal molecules binding to receptors, triggering second messengers and signal transduction pathways. Metabolism encompasses catabolic (energy-releasing) and anabolic (energy-requiring) pathways, regulated by energy carriers like ATP, NADH, and acetyl-CoA. Glycolysis converts glucose to pyruvate, generating ATP and NADH, while gluconeogenesis synthesizes glucose from non-carbohydrate precursors. The citric acid cycle and electron transport chain complete aerobic respiration, maximizing ATP production.