lecture 1 Flashcards

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1
Q

what are the main macromolecules

A

proteins, carbs, lipids, and nucleic acids

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2
Q

what are polymers? what are they made up of?

A

any of a class of natural or synthetic substances composed of very large molecules called monomers

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3
Q

what are the enzymes that make polymers? what is the reaction called? what kind of rxn is this? what is the opposite of the rxn?

A

polymerases, polymerization, dehydration or condensation rxn, and hydrolysis rxn

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4
Q

what is the monomer of proteins? how many AA’s are there?

A

amino acids and there are 20 AA’s

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5
Q

In mutation notation what does R322K mean?

A

R is the good AA that should be there 322 is the position or location of mutation, and K is the mutant AA or the changed AA

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6
Q

would a change from R to K AA be a big deal?yes or no

A

no because both are polar positive AA’s

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7
Q

what is C terminus what is N terminus? what is a polypeptide held by?

A

C terminus is the free carboxyl group and N is the free amino group at the ends of a polypeptide. it is held by a peptide bond

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8
Q

where do you add an AA to a polypeptide chain?

A

always add to C terminus

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9
Q

how are AA’s synthesized? (direction of peptide)

A

from N to C

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10
Q

primary structure and secondary structure

A

primary: AA sequence secondary: Hydrogen bonding between backbone atoms of the AA’s, formation of alpha helices and beta sheets

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11
Q

tertiary structure and quaternary structures

A

tertiary: folding of protein due to the SIDE CHAIN interactions within a polypeptide like nonpolar nonpolar bonds, acid/base electrostatic bonds, etc quaternary: side chain interactions between DIFFERENT polypeptidechains

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12
Q

what are the three non covalent bonds seen in AA’s? covalent?

A

non covalent: nonpolar to nonpolar, polar neutral to polar neutral, and acid base bonds.
covalent: disulfide bridges

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13
Q

what are some protein functions

A

transporters, hormones, cell signaling, receptors, muscles

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14
Q

what are carbs with one sugar called? what is the monomer of carbs?

A

answer to both questions: monosaccarides

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15
Q

what is the formula for carbs

A

CnH2nOn

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16
Q

what are the three most common monosacc. and what is the formula for them (6c)

A

glucose, fructose, and galactose, all have six carbons so formula C6H12O6

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17
Q

what are the two common 5c monosacc

A

ribose and deoxyribose C5H10O5

18
Q

what are the three most common disacc and what are they made of ? what is the formula of these disacc

A

maltose: glucose + glucose sucrose: glucose + fructose lactose: glucose + galactose, formula C12H22O11

19
Q

what is important to note about the condensation rxn between monosaccs into disacc or polysacc

A

you ALWAYS release H20 so in the formula you must always subtract 2 hydrogens and 1 oxygen

20
Q

common polysacc and their functions

A

glycogen: animal glucose storage starch: plant glucose storage cellulose: plant structure

21
Q

what is the monomer for a lipid? what is special about this monomer

A

hydrocarbon, it is very hydrophobic

22
Q

what makes a saturated fatty acid and what is its property

A

no double bonds present, all carbons are bonded with as many hydrogens as they can and it is solid at room temp due to being DENSELY PACKED

23
Q

what makes a saturated fatty acid and what is its property

A

double bonds present, double bonds causes kinks in the structure causing more fluidity. liquid at room temp because it cannot be densely packed due to kinks

24
Q

triglycerides are made up of what? what kind of bond do they have between their pieces?

A

sugar/glycerol back bone with fatty acids are condensed causing release of water making an ester bond through esterification

25
Q

what are phospholipids made up of? what is special about this molecule

A

sugar/glycerol back, fatty acid, and a phosphate group. they are special because they are amphiphilic OUTSIDE hydroPHILIC INSIDE hydroPHOBIC

26
Q

what are terpenes made up of what? how do you name terpenes? where do you find terpenes

A

terpenes are made up of isoprenes (hydrophobic unit), you name them by counting how many pairs you see, three pairs (six isoprenes) would be names triterpene, you find these in waxes

27
Q

steroids come from what?

A

cholesterol

28
Q

what does cholesterol look like

A

3 six carbon rings with 1 five carbon ring

29
Q

what is delta g, delta h, and delta s

A

delta g is gibbs free energy, delta h is enthalpy or potential energy and delta s is entropy or kinetic energy

30
Q

what is delta g less than 0? greater than 0? equal to 0?

A

less than 0= spontaneous rxn favorable, greater than 0= nonspon rxn unfavorable, and equal to 0 is equilibrium

31
Q

what is reaction coupling

A

if one equation is unfavorable, you can add a big favorable rxn with a very negative delta g that when added with the positive delta g, it is still negative make it favorable

32
Q

what is a transition state? what is energy of activation?

A

transition state is a transient high energy state in between reactants and products, the activation energy of a rxn is the energy needed to produce transition state. you make a rxn fast by lower activation energy

33
Q

how do catalysts work? what is important to note about catalysts?

A

they work by 1. stabilizing transition state and 2. reduce activation energy, CATALYSTS DO NOT AFFECT DELTA G OF A RXN

34
Q

what are the three defining characteristics of enzymes

A
  1. must increase the rate of the rxn 2. must not be used up in the rxn 3. specific for a particular rxn
35
Q

how can you turn the t state into the r state? what is r state? what is t state?

A

phosphorylation and allosteric regulation. r state ON is the relaxed state when affinity to substrates is higher, t state OFF is the tense state in which enzyme does not want to bind to substrate

36
Q

what is vmax? km?

A

vmax is when the enzyme is full saturated with enzyme so graph begins to plateau. km is when the substrate is half of vmax

37
Q

competitive inhibition? what is vmax and km? what does LWB plot look like?

A

binds at active site, vmax: unchanged km: increased, lines cross at y axis

38
Q

noncompetitive inhibition? what is vmax and km? what does LWB plot look like?

A

binds at allosteric site, does not change the shape of active site but doesnt allow ES complex to form vmax: decreased km: unchanged, and graph starts at the same point on x axis

39
Q

uncompetitive inhibition? what is vmax and km? what does LWB plot look like?

A

binds at allosteric site of ES complex not allowing the substrate to go. vmax and km decreased, graph looks like parallel lines not touching

40
Q

mixed inhibition

A
  1. can bind to the allosteric site of enzyme alone cause km to be increased or 2. can bind at ES complex causing km to be decreased, either way vmax is decreased in both
41
Q

x intercept of LWB P and y intercept of LWB P

A

x int: is -1/km and y int: 1/vmax