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
physical conditions affect enzyme function
temp or pH shifts denaturation = unfolding -- nonfunctional
26
changes on protein structure & function if amino acid is changed
change in primary structure does not have to change everything, but it can
27
what happens if you swap a hydrophobic amino acid for hydrophilic in primary structure
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
saturated fatty acid
animal fats straight no double bond pack tightly, solid at room temp, less fluid increases level of LDL
29
unsaturated fatty acids
plant fats double bond causes bending loosely packed, liquid at room temp, more fluid decrease in LDL, increase in HDL
30
LDL
low density lipoprotein carries cholesterol from liver to cells "bad" cholesterol you need some but a lot can clog ur arteries
31
HDL
high density lipoprotein more apo proteins picks up extra cholesterol from cells delivers to liver for disposal / recycling "good" cholesterol
32
cis vs trans fat
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
explain why phospholipids form bilayers while triglycerides form insoluble droplets
phosolipids - hydrophobic tails & hydrophilic heads, put tails together on inside & heads on outside triglycerides - very hydrophobic