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Functional Groups and macromolecules
Almost all chemicals of life are carbon based ◦ Except water
Compounds containing carbon are referred to as organic compounds ◦ Except carbon gases such as CO2
Organic compounds where originally believed to be made through biological processes ◦ Petrochemical and bioengineering now make a
variety of organic compounds
Carbon is able to make four stable covalent bonds with other atoms
The symmetry of bonding makes most molecules non-polar
Molecules composed solely of carbon and hydrogen
Other organic compounds contain one or more extra element in a functional group
Small groupings of elements, normally found near the end of a large organic molecule, that gives the molecules special reactive/bonding properties
normally composed of H, O, P, N and S
These groups are mainly polar and will make that end of the molecule more reactive and able to form new bonds
Aspirin
Try practice on pg. 27
Large Repeating subunits (usually) Four classes ◦ Lipids, carbohydrates, proteins, nucleic acids
Polymers (c, p, na) ◦ Assembled via energy absorbing condensation
reaction (dehydration synthesis) – anabolic reaction!
◦ Broken down into subunits (catabolic reaction) via hydrolysis, releasing energy
◦ Both of these use enzymes to make reaction more efficient
Produced via photosynthesis
Used by organisms for energy, building materials, id markers (e.g. blood types)
C:H:O ratio 1:2:1
Mono, oligo, and polysaccharides
“ose” ending ◦ triose, pentose, hexose
Isomers same formula different shape
Mono - glucose, ribose, fructose, galactose
Oligo – maltose, sucrose, lactose
Poly – glycogen (branched), cellulose (straight), chitin (straight), starch (amylose – straight, amylopectin – branched)
Storage ◦ Animals – glycogen Stored in muscle and liver, 1 day supply
◦ Plants – starch Plants produce more glucose than necessary for their needs,
chloroplasts make starch, stored in plastids, tubers, taproots and grain fruits
Consumed by animals for food
Structure ◦ Plants – cellulose Plant cell walls (most abundant organic substance on Earth!) Usefulness to us – clothing, wood and paper products, Requires bacteria for breakdown (cows, sheep, rabbits…) Fibre!!!
◦ Animals – chitin (insect and crustacean exoskeletons), fungi Usefulness to us – contact lenses, biodegradable stitches
C, H, O Hydrophobic - more non-polar bonds than
carbs ◦ Insoluble in water, soluble in non-polar substances
Used for storing energy, building cell parts, and for signaling
4 families ◦ Fats, phospholipids, steroids, waxes
Twice the energy storage of carbs
Excess carbs are stored as fats in animals and plants ◦ Triglycerides – ester linkages
Saturated vs. unsaturated
Animal vs. plant fats
Saturation allows for more intermolecular bonding, therefore solid at room temperature
Hydrogenation of plant oils
Margarine vs. butter vs. oil debate!
Cell membranes Phosphate, glycerol, 2
fatty acids Polar head
(hydrophilic), non-polar tails (hydrophobic)
Micelles Lipid bilayers ◦ proteins and pores
required for charged substances to pass through non-polar tails
4-Ring structures with functional groups
E.g. Cholesterol ◦ Atherosclerosis – plaque (fatty deposits) in arteries
blocks blood flow
◦ Converted into vitamin D and bile salts
E.g. Sex hormones – estrogens, testosterone, progesterone
Fatty acids linked to alcohol or carbon rings
Hydrophobic ◦ Waterproof coatings
Cutin (cuticle) on plant surfaces
Birds, bees, …
Most diverse and important molecules
DNA codes for proteins
Uses ◦ Enzymes – reactions at life-sustaining speeds
◦ Immunoglobulins - protection
◦ Transport – membrane proteins, hemoglobin
◦ Structure – keratin in hair and nails, fibrin in blood clots, collagen in bones/skin/etc.
Amino acid polymers folded into 3D shapes ◦ Amino acid – R group, carboxyl group, amine
group 20 different amino acids 8 essential amino acids – not synthesized by body
◦ Conformation is determined by amino acid sequence (polypeptide) Linkage between amino acids is called peptide bond Also formed by condensation reaction Amino group at one end (A-terminus), carboxyl group at
the other end (C-terminus)
◦ Polypeptide is made in cytoplasm via protein synthesis, according to DNA instructions
Meet the amino acids – pg. 42
Linear or sheet proteins - structural
Globular proteins – enzymes/functional ◦ Primary structure – aa sequence, one change can alter
function (eg. Sickle cell anemia) ◦ Secondary structure – coils and folds in the original aa
chain due to H bonds, alpha helix or beta pleated sheet ◦ Tertiary – environmental forces that cause additional
folding (eg. Hydrophobia, polar/non-polar R groups) A polypeptides final shape
H bonds, ionic bonds, van der Waals forces, disulfide bridges
◦ Quaternary – clustering of 2 or more polypeptides A proteins final shape
Determined by primary structure and environment
http://users.rcn.com/jkimball.ma.ultranet/BiologyPages/D/Denaturing.gif
Proteins are made in a certain environment Temp, pH, ionic [ ], etc. can change shape
(denature) H bonds, ionic bonds, disulfide bridges etc. will all
return to normal once change is reversed in small proteins
Chaperone proteins aid in folding Peptide bonds will not be remade however, so if
that occurs, protein is irreparably damaged Useful denaturation ◦ Gastrin denatured by SI pH ◦ Salt, sugar, vinegar denature food spoiling enzymes ◦ Blanching denatures browning enzymes ◦ Heat denatures hair proteins for shape changes ◦ Cooking meat for easier eating