molecules - exam 1 Flashcards

1
Q

covalent bond

A

involves sharing of electron pairs between atoms

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2
Q

nonpolar

A

share electrons equally

no charge

CC & CH bonds

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3
Q

polar

A

don’t share electrons equally

partial charge

water soluable

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4
Q

polar covalent bonds important in molecules

A

OH
NH
SH

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5
Q

hydrogen bond

A

attraction of partial charges (positive & negative)

break easily – that’s why water is fluid

water can H bond to other polar molecules but not other H20

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6
Q

why can salt dissolve in water & oil can’t

A

salt is polar - polar molecules are water soluble

oil is nonpolar - water can’t break down its bonds

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7
Q

hydrolysis

A

water in, monomer out

using water to break a bond in a molecule

need hydrolytic enzymes

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8
Q

dehydration synthesis

A

monomer in, water out

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9
Q

monosaccharide

A

monomer

single subunit

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10
Q

disaccharide

A

dimer

2 monomers

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11
Q

polysaccharide

A

many monosaccharides

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12
Q

oligosaccharide

A

carbohydrate comprised of a relatively small number of monosaccharides

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13
Q

starch

A

function: energy storage in covalent bonds

found in plants

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14
Q

glycogen

A

function: energy storage in muscle & liver cells

found in animals & fungi

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15
Q

cellulose

A

function: structural

found in the cell wall of plants, helps them stay upright

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16
Q

chitin

A

structural

17
Q

how can cows digest cellulose

A

they have a special bacteria that can break down cellulose & then the bacteria eats it

18
Q

primary structure

A

sequence of a chain of amino acids

amino end & carboxyl end

“2D”

19
Q

secondary structure

A

localized folding created by hydrogen bonding

interactions between R-groups

still “2D”

20
Q

tertiary structure

A

3D shape

interactions between r groups maintain structure

central carbons on polypeptide backbone
r groups bond via h bonds, ionic bonds, covalent bonds, hydrophobic exclusion – giving it curly shape

blob of curly ribbon

21
Q

chaperones

A

help proteins fold in the proper way (tertiary)

22
Q

quaternary structure

A

aggregation of 2 or more polypeptides

separate they don’t work, together they do

23
Q

substrate

A

what is going to be acted on by enzyme

24
Q

enzyme substrate complex

A

enzyme = active site

substrate (2 molecules bonded) enters enzyme

H2O added to reaction

enzyme breaks down bond & produces 2 products

25
Q

physical conditions affect enzyme function

A

temp or pH shifts

denaturation = unfolding – nonfunctional

26
Q

changes on protein structure & function if amino acid is changed

A

change in primary structure does not have to change everything, but it can

27
Q

what happens if you swap a hydrophobic amino acid for hydrophilic in primary structure

A

primary structure will be changed - completely different amino acid

will also change 2nd, 3rd, 4th structures (& maybe function) because the proteins will have to fold differently

28
Q

saturated fatty acid

A

animal fats

straight

no double bond

pack tightly, solid at room temp, less fluid

increases level of LDL

29
Q

unsaturated fatty acids

A

plant fats

double bond causes bending

loosely packed, liquid at room temp, more fluid

decrease in LDL, increase in HDL

30
Q

LDL

A

low density lipoprotein

carries cholesterol from liver to cells

“bad” cholesterol
you need some but a lot can clog ur arteries

31
Q

HDL

A

high density lipoprotein

more apo proteins

picks up extra cholesterol from cells
delivers to liver for disposal / recycling

“good” cholesterol

32
Q

cis vs trans fat

A

cis - unsaturated is best for you, bent
hydrogen & carbon on same side of double bond

then saturated

then trans unsaturated
hydrogens & carbons on opposite side of double bond
partially hydrogenated

33
Q

explain why phospholipids form bilayers while triglycerides form insoluble droplets

A

phosolipids - hydrophobic tails & hydrophilic heads, put tails together on inside & heads on outside

triglycerides - very hydrophobic