Organic Chemistry Intro

University:
Princeton University
Course:
PHY 103 | General Physics I
Academic year:

2023
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0

Pages:

5
Author:

customer-8086373

BIOCHEM: SBI4U1 Organic Chemistry Intro Functional Groups Reactions: 1. Dehydration synthesis (condensation reactions) a. Removes a water molecule and forms a covalent bond between monomers i. One monomer provides a hydroxyl group and the other provides a hydrogen and together they form water. 2. Hydrolysis (opposite of dehydration synthesis) a. Covalent bond is broken between monomers in the polymer b. A hydrogen atom and a hydroxyl group from a split water molecule attaches where the covalent bond use to be Macromolecules Carbohydrates 1. Monosaccharides: simple sugars 2. Disaccharides: double sugar (two monosaccharides joined by condensation reaction) 3. Polysaccharides: polymers of monosaccharides - - - - Carbohydrates are an immediate source of fuel Most names for sugars end in -”ose” Classified by the number of carbons and the location of the carbonyl group Isomers have the same molecular formula but differ in structural arrangements Monosaccharides - Carbonyl group - Hydroxyl groups Ex. glucose, fructose - Classified by the number of carbons in the backbone - Glucose and other six carbon sugars are hexoses - Five carbon backbones are pentoses and three carbon sugars are trioses Disaccharides - Formed from two monosaccharides joined by a glycosidic linkage (ether group: 2 hydroxyls) Ex. glucose + fructose → sucrose + water Polysaccharides (storage) - Polymers of hundreds to thousands of monosaccharides joined by glycosidic linkages - Function in energy storage Ex. starch - Composed of entirely glucose monomers with 1-4 linkages - Amylose: unbranched, forms helix - Amylopectin: branched, more complex Glycogen - Animal storage molecule - Highly branched like amylopectin - Humans store glycogen in liver and muscles (only have a one day supply) Beta glucose vs Alpha glucose Starch - polysaccharide of alpha glucose monomers Cellulose - polysaccharides of beta glucose monomers (with beta rings) Polymers built with alpha glucose form helical structures Polymers build with beta glucose form straight structures - Most Beta linkages are unable to be broken down in the body and are excreted as waste in feces Lipids - Monomer is the fatty acid - Fats, oils, waxes - Hydrophobic (DO NOT dissolve in water) - Long term energy storing molecule - Lipids have double the energy per gram than carbs 4 types of lipids 1. Fatty acid: long hydrocarbon chain with carboxyl group on end a. Saturated: fully hydrogenated (hydrogen at every position), straight chain i. Solid at room temp, may contribute to cardiovascular disease b. Unsaturated: double/triple bonds where hydrogen is missing, bent structure at double/triple bonds i. Liquid at room temp, plant and fish fats (oils) 1. MUFA (monounsaturated fatty acids, one double bond) 2. PUFA (polyunsaturated fatty acid, more than one double bond) 2. Fats & Oils: lipids used to store energy (formed by combining 3 fatty acids + glycerol) a. Cushions vital organs, functions as insulation b. Triglyceride - 3 fatty acids joined to a glycerol by ester linkage 3. Phospholipids: composes the cell membrane bilayer a. Have 2 fatty acids attached to glycerol and phosphate group b. Fatty acid tails are hydrophobic c. Phosphate group and other attachments form a hydrophilic head d. When interacting with water, they self-assemble into a structure with the hydrophobic tails in the center and the hydrophilic heads on the outside (phospholipid bilayer) 4. Steroids: differ from other lipids in structure, serve as hormones Proteins Amino acids There are 20 amino acids Structure of amino acids 1. Primary structure: one line of amino acids code 2. Secondary structure: helix formation 3. Tertiary structure: pleated sheet is added into the amino acid mix 4. Quaternary structure: 3d blob Membranes and Transport - Barrier only allows gasses like oxygen and carbon dioxide to cross and some other small nonpolar molecules Glycoproteins: provide a site for cell to cell attachment or attach to lipids (glycolipids) as cell identification tags. (vital for immune response) Receptor proteins: have specific shapes to detect signal molecules (hormones) and pass on information 1. Passive transport (diffusion): movement of molecules from an area of high concentration to an area of low concentration (high → low) with the concentration gradient. No ATP is needed a. Ex. water, carbon dioxide, oxygen, small lipid molecules, lipid soluble molecules (alcohol) 2. Protein facilitated diffusion (passive transport): moves specific molecules that cannot move directly through the membrane with the concentration gradient Integral proteins 1. Transporter 2. Receptor 3. Enzyme OSMOSIS!!!!!!!!!!!!! - Water diffuses constantly through aquaporins or water sensitive membrane regions 1. Hypertonic (shrunk) more water outside the cell than inside (in < out) 2. Isotonic (normal) equilibrium (equal amounts of water inside and outside) (in = out) 3. Hypotonic (swollen) more water inside the cell than outside (in > out) Water will always flow to the side of the membrane with a higher solute concentration Turgor pressure (in plants) Hypertonic - plasmolysis (lack of water causes cell to shrink away from cell wall) Isotonic - flaccid Hypotonic - turgid (favourable) Active transport - Against the concentration gradient, requires ATP - Molecules too big or hydrophilic to pass through membrane Bulk transport (form of active transport) 1. Uses cell membrane to create transport vesicles that can engulf or empty large amounts of cellular material at once (endocytosis - engulfing and transporting cellular material | exocytosis - transporting cellular waste/ molecule secretion and releasing it) 2. Types of endocytosis - phagocytosis: engulf solids and whole cells | pinocytosis: engulf liquids | receptor mediated endocytosis: molecules bind to surface receptors that trigger engulfment by membrane Enzymes Enzymatic reaction - molecules in beginning are substrates → products Some enzymes require an activator to attached to their allosteric site for the active site to be receptive to the substrate - Competitive inhibitors: inhibitor competes with substrate for access to active site of enzyme - Non-competitive inhibitors: substances attach to the allosteric site and change shape of active site to prevent substrate from binding to it Irreversible inhibition Competitor: permanently binds to active site Allosteric: permanently binds to allosteric site, permanently changes shape of enzyme