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Core I > Exam I > Flashcards

Exam I Flashcards

1
Q

equilibrium

A

extent of rxn, how much is made or foormed

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2
Q

1st law of thermo

A

energy neither created nor destroyed

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3
Q

enthalpy

A

heat exchange, H

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4
Q

delta H > 0

A

exothermic, gives off heat

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5
Q

H<0

A

endothermic, takes in heat

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6
Q

2nd law

A

entroypy is always inceraseing S, randomness/disorder

more favorable to increase S

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7
Q

s<0

A

binding

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8
Q

s>0

A

releaese

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9
Q

free energy eq

A

delta G=deltaH-T*DeltaS

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10
Q

G

A

favorable, spont, exergoninc

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11
Q

G>0

A

unfav, nonspont, edergonic

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12
Q

G=0

A

@ equilibrium

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13
Q

k

A

[prod]/[react]

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14
Q

deltaG*

A

-RTln(k)

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15
Q

is hydrophobic effect favorable

A

no but happens anyway

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16
Q

pI

A

pH when net charge = 0

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17
Q

pH

A

net pos

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18
Q

pH>pI

A

net neg

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19
Q

formation of salt bridges

A

stabalizes T state and releases O

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20
Q

adding enzyme to rxn at equilibrium

A

doesnt change concentrations of s or p

only changes rate of reaching eq

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21
Q

do reaction starting with product and enzyme

A

still same [] because rxns are reversible

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22
Q

glutamate charge at neutral ph

A

-1

23
Q

pka vs ph trends

A

pHpKa is negative

24
Q

know the titration curve

A

pH is y axis so bases start high and end low or reverse x axis

25
Q

entropy change with hydrophobic in water

A

delta s is negative because the water becomes more ordered as it goes around the compound

26
Q

sugar code

A

micro-heterogeneity
building blocks of sugar molecules
basically like how monosaccharides can bind in different ways and still be sugars but have different func
ex. protein lectin is read by cells or pathogens for immunitiy or infection and not for energy

27
Q

amylose vs cellulose

A

anomers, orientation differs at one carbon.
amylose is digestible
cellulose is like cell wall of plants and is not

28
Q

subunits of HIV-1 ENV spike

A

Cap - gp-120 - 3 of them

spike - gp-41 - 3 of them

29
Q

what binds in HIV

A

gp120 binds w. CD4 on host cell

30
Q

conform changes in HIV binding

A

gp120 bind CD4 making complex with change that activates gp41’s helical bundles to fuse into the cell membrane

31
Q

exp method to determine AA side chains in ENV bind to receptors

A

mutagenesis: sequence coding for one side chain at a time

is translated and replicated in the host cell

32
Q

spr

A

d

33
Q

itc

A

d

34
Q

5’ end of DNA

A

has the phosphate group on the 5th carbon attatched to carbon 4 or the ring

35
Q

3’ end of DNA

A

just has an O coming off the third with anomeric C as number 1 (where base is bound)

36
Q

purines

A

adenine and guanine

37
Q

adenine

A

two rings and 2 h bonds to thymine

38
Q

guanine

A

two rings and 3 binds to cytosine

39
Q

pyrimidines

A

cytosine and thymine (and Uracil)

40
Q

cytosine

A

one ring 3 binds to guanine

41
Q

thymine (and Uracil)

A

one ring and 2 binds to Adenine

42
Q

nitroginous base pairs

A

AT

GC

43
Q

phosphodiester bonds

A

between 3’ and 5’

44
Q

bases vs sugars in dna

A

bases link strands

sugars compose backbone

45
Q

why uracil is used in RNA not DNA

A

DNA glycosides edit DNA and would mistake uracil for degraded (deaminated) cytosine and remove it but thymine is different enough to prevent this

46
Q

most common form of dsDNA

A

B

47
Q

hydrophobic effect in dsDNA

A

twist from h-bonds between nitrogenous bases,

keeps hydrophobic bases protected by phosphate-sugar backbone

48
Q

pi energy electro static forces

A

how does it stabalize base stacking??

helps solvent channel and helical structure>

49
Q

3rd energetically favorable force in dsDNA form?

A

j

50
Q

RNA flexibility, why

A

wobble base pairing different combos

hoogsten base pairing different angles?

51
Q

2 RNA functions

A

catalityic - ribozymes cleave circular DNA

machine - ribosome make proteins like tRNA and rRNA

52
Q

chris anfinson

A

foudn ribonuclease that protein folding is inherent in AA structure

53
Q

anfinsens cage and GroES/GroEL

A

are chaperone proteins that showed that in vivo would have same inhereint folding of proteins as in vitro

Core I (6 decks)

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