3.2-6 macromolecules Flashcards by Kate McNamara

monomers definition

small organic
used for building blocks of polymers
connects with condensation reaction (dehydration synthesis)

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polymers definition

long molecules of monomers
many identical or similar blocks linked by covalent bonds

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macromolecules

giant molecules
2+ polymers bonded together

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dehydration synthesis (condensation reaction) properties

make polymers
monomers –> polymers
A + B –> AB
produces H2O

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hydrolysis properties

breakdown polymers
polymers –> monomers
AB –> A + B
uses H2O

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hydrolysis definition

breaking down a polymer

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carbohydrates properties

fuel and building material
includes simple sugars (fructose) and polymers (starch)
ratio: CH2O

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monosaccharides definition

monomers

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polysaccharides purpose

storage (plants-starch, animals-glycogen)
structure (plant-cellulose, arthropod-chitin)

differs in position and orientation of glycosidic linkage

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two types of glucose

starch: α glucose
cellulose: β glucose

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structural polysaccharides

cellulose and chitin (exoskeleton)

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fats/oils (triglyceride) purpose and properties

store energy
glycerol (3C alcohol) + 3 fatty acids
saturated, unsaturated, polysaturated

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steroids structure

4 fused carbon rings (isoprene) + ??

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how are different steroids created?

attaching different functional groups to rings

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different structure creates

different function

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phospholipid structure

glycerol + 2 fatty acids + PO4

hydrophobic fatty acid tails
hydrophilic PO4 head

steroid backbone

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hydrophobic/hydrophilic interactions create

phospholipid bilayer

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waxes are made up of

glycerol and alcohol (monomer)

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nucleic acid function

store hereditary info

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DNA properties

Double-stranded helix
N-bases: A, G, C, Thymine
Stores hereditary info
Longer/larger
Sugar: deoxyribose

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RNA properties

Single-stranded
N-bases: A, G, C, Uracil
Carry info from DNA to ribosomes
tRNA, rRNA, mRNA, RNAi
Sugar: ribose

various functions during gene expression

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nucleotide definition

monomer of DNA/RNA

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nucleotides are made of

sugar + phosphate + nitrogen base

information flow in a cell

DNA –> RNA –> protein

proteios meaning

first or primary

proteins contain what elements?

c, h, o, n, s

proteins take up what percentage of dry weight in a cell?

50%

proteins functions

enzymes defense storage transport hormones receptors movement structure

enzymatic protein function

selective acceleration of chemical reactions

defensive proteins function

protection against disease

storage proteins function

storage of amino acids

transport proteins function

transport of substances

hormonal proteins function

coordination of an organism's acitivities

receptor proteins function

response of cell to chemical stimuli

contractile and motor protein functions

movement

structural proteins function

support

primarily level of protein structure

amino acid sequence 20 different amino acids

what bonds link amino acids?

peptide bonds

amino acid properties

hydrophobic non polar r-group hydrophilic polar r-group ionic (acids and bases)

amino acid

r-group: side chains amino: -NH2 acid: -COOH

secondary level of protein structure

3d shape hydrogen bonding between oxygen of carboxyl of one amino acid and hydrogen of another

what shapes does the secondary level of protein structure form?

Alpha (α) helix, Beta (β) pleated sheet

4 basic principles of protein folding

Hydrophobic/nonpolar amino acids buried in interior of protein (hydrophobic interactions) Hydrophilic/polar amino acids exposed on surface of protein (hydrogen bonds) Acidic and basic amino acids form salt bridges (ionic bonds) Cysteines can form disulfide bonds

tertiary level of protein structure

bonding between r-groups (side chains) of amino acids

tertiary level of protein structure bonds

hydrogen ionic disulfide bridges van der Waals interactions

quaternary level of protein structure

2 or more polypeptides bonded together

amino acid process

amino acid --> polypeptides --> protein

chaperoning purpose

assist in proper protein folding

protein _ and _ are sensitive to chemical and physical conditions

structure, function

what conditions are not optimal for proteins?

changes in pH and temperature

what happens if proteins are restored to original conditions after changes in temp or pH?

renaturation or permanent denaturing

carbohydrates components

C, H, O

carbohydrates examples

mono, di, polysaccharides

carbohydrates functions

fuel: carbon sources that can be converted to other molecules or combined into polymers strengthen plant cell walls stores glucose for energy strengthens exoskeletons and fungal cell walls

lipid examples

triacylglycerols phospholipids steroids

lipids functions

important energy source lipid bilayer component of all cell membrane (cholesterol) signaling molecules that travel through the body (hormones)

proteins components

amino and monomer (20 types)