Biomolecules Overview Amino Acids Structure : Alpha-carbon attached to carboxylate (-COO⁻), protonated amino group (-NH₃⁺), hydrogen, and side chain (R group).Zwitterions : Exist at physiologic pH; neutral molecule with equal positive and negative charges.Classification : By R group polarity: Hydrophobic (nonpolar), Polar (neutral), Negatively charged (acidic), Positively charged (basic).Nonpolar, aliphatic : Glycine, Alanine, Valine, Leucine, Isoleucine, Methionine, Proline.Aromatic : Phenylalanine, Tyrosine, Tryptophan.Polar, uncharged : Serine, Threonine, Cysteine, Asparagine, Glutamine.Positively charged : Lysine, Arginine, Histidine.Negatively charged : Aspartate (Asp), Glutamate (Glu).Hydrophobic R groups : Sequestered inside protein cores.Hydrophilic R groups : Interact with water on protein surfaces.α-Amino Acids : Amino group adjacent to the carboxylate group; 19 of 20 are stereoisomers (glycine is achiral).4 Levels of Protein Structure Primary : Sequence of amino acids linked by covalent peptide (amide) bonds (-CO-NH-).Secondary : Local folding into regular 3D structures (α-helix, β-pleated sheet) stabilized by hydrogen bonds between backbone –NH– and –C=O– groups.Tertiary : Overall 3D shape of a single polypeptide chain, maintained by side-chain interactions (salt bridges, H-bonds, hydrophobic interactions, disulfide bridges).Quaternary : Arrangement of multiple polypeptide subunits, maintained by same forces as tertiary structure.Collagen : Most abundant protein; three chains (tropocollagen) held by H-bonds; rich in glycine.Denaturation of Proteins Loss of organized conformation (higher-order structures) due to temperature, pH extremes, solvents, etc.; primary structure remains intact. Lipids: Biological Functions and Classification Functions : Energy source (\sim 9 kcal/g), membrane structure, hormones, lipid-soluble vitamins, shock absorption, insulation.Classes : Fatty Acids, Glycerides, Nonglyceride lipids (sphingolipids, sterols, waxes), Complex lipids (lipoproteins).Fatty Acids Long, straight-chain carboxylic acids (10–20 carbons), can be saturated or unsaturated. Unsaturated fatty acids : Have double bonds (cis) that decrease melting temperature by preventing tight packing.Glycerides Glycerol esterified with fatty acids. Triacylglycerols (TAGs) : Three fatty acids to glycerol; energy storage in adipose tissue.Oils = unsaturated TAGs (liquid); Fats = saturated TAGs (solid). Hydrogenation : Adding H_2 to convert unsaturated to saturated facts.Saponification : Base-catalyzed hydrolysis of TAGs to glycerol + fatty acid salts (soap). Soaps form micelles.Micelles, Liposomes, and Bilayers Micelle : Spherical; hydrophobic tails inward, hydrophilic heads outward.Liposome : Bilayer vesicle with aqueous interior.Bilayer : Planar sheet of phospholipids; basic membrane structure.The Cell Membrane Lipids : Phospholipids, glycolipids, sterols.Cholesterol : Common sterol; modulates membrane fluidity/rigidity; precursor to steroid hormones.Membrane proteins : Integral (span membrane) and Peripheral (surface).Bile Acids Synthesized from cholesterol in the liver; amphipathic; form micelles to emulsify fats in the intestine. Steroid Hormones Classes : Mineralocorticoids (e.g., aldosterone), Glucocorticoids (e.g., hydrocortisone), Sex hormones (e.g., testosterone, estradiol).Eicosanoids Derived from arachidonic acid (essential fatty acid). Families : Prostaglandins, Leukotrienes, Thromboxanes.Functions : Regulate inflammation, vasoconstriction, platelet aggregation.Aspirin : Inhibits prostaglandin synthesis by acetylating cyclooxygenase (COX).Complex Lipids: Lipoproteins Transport lipids in blood; neutral lipid core (cholesterol esters/TAGs) surrounded by phospholipids, cholesterol, and protein. Classes : Chylomicrons (gut to adipose), VLDL (liver to tissues), LDL (cholesterol to tissues), HDL (scavenges cholesterol).LDL receptor : Defects linked to familial hypercholesterolemia.Carbohydrates and Glycoconjugates Structure : Biomolecules with multiple –OH groups and aldehyde/ketone.Types : Monosaccharides (e.g., glucose, fructose), Disaccharides (e.g., sucrose, lactose) linked by glycosidic bonds, Oligosaccharides (3-10 monosaccharides), Polysaccharides (long chains like starch, glycogen, cellulose).Monosaccharide Naming : Aldose (aldehyde) vs. Ketose (ketone), Triose (3C) to Hexose (6C).Chirality : Many chiral carbons create stereoisomers; 2^n possible for n chiral centers.Disaccharides : Sucrose (glucose + fructose), Lactose (galactose + glucose, \beta(1\to 4)), Maltose (glucose + glucose, \alpha(1\to 4)).Polysaccharides : Homopolysaccharides (single monomer): Chitin (N-acetylglucosamine, \beta(1\to 4)), Cellulose (glucose, \beta(1\to 4), strong structural), Starch (amylose-linear, amylopectin-branched, \alpha(1\to 4), \alpha(1\to 6) storage in plants), Glycogen (highly branched \alpha(1\to 4), \alpha(1\to 6) storage in animals).Glycoconjugates : Proteoglycans (protein + sulfated glycosaminoglycans), Glycoproteins (protein + branched carbohydrate chains), Glycolipids (lipid + carbohydrate).Blood Groups : Determined by oligosaccharide antigens on erythrocyte surface glycoproteins.Nucleic Acids Types : DNA (store/transmit genetic info) and RNA (protein synthesis).Nucleotide Structure : Nitrogenous base (Purines: A, G; Pyrimidines: C, T, U), pentose sugar (deoxyribose/ribose), phosphate group.DNA Structure : Double helix; sugar–phosphate backbone outside, bases stacked inside. Antiparallel strands (5′→3′, 3′→5′). Base pairing: A-T (2 H-bonds), G-C (3 H-bonds).Transcription (DNA to RNA) : RNA complement to DNA template; U replaces T.Translation (RNA to protein) : mRNA codons read by ribosome; tRNA brings amino acids.Central Dogma : DNA \to RNA \to Protein (with DNA replication), describing the flow of genetic information.Peptide bond: -C(=O)-NH- TAG saponification: Triacylglycerol + 3 NaOH \to glycerol + 3 RCOONa DNA base pairing: A-T (2 H-bonds), G-C (3 H-bonds) Transcription example: If DNA is AATTGCGC, mRNA is UUAACGCG. Knowt Play Call Kai