chem exam 3 Flashcards

1
Q

PH < 2

A

both protonated (have H), charge of +

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2
Q

pH 7.4 neutral

A

C deionized; NH protonated, charge of 0

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3
Q

ph > 10

A

both deprotonated (don’t have H), charge of -1

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4
Q

A and T

A

2 bonds

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5
Q

C and G

A

3 bonds

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6
Q

base hydrolysis

A

carboxylate salt and amine

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7
Q

acid hydrolysis

A

carboxylic acid, protonated amine

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8
Q

disulfide bonds

A

thiol (s)

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9
Q

peptide bonds (amide bonds)

A

between amino acids

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10
Q

hydrophobic interactions

A

hydrocarbon R groups

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11
Q

salt bridges

A

ionic bonds, acid/base

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12
Q

hydrogen bonds

A

OH

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13
Q

allosteric

A

different bonding site

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14
Q

inhibitor

A

stop reaction from occurring

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15
Q

competitive inhibitor

A

binds to the active site so reaction cant occur

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16
Q

noncompetitive inhibitor

A

binds to an allosteric site to change the shape so no reaction can occur

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17
Q

nucleoside

A

sugar + base

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18
Q

nucleotide

A

sugar + base + phosphate

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19
Q

amine as a base

A

gains proton

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20
Q

NH4 shape

A

tetrahedral

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21
Q

NH3 shape

A

trigonal pyramidal

22
Q

heat denatures

A

hydrogen bonds and hydrophobic interactions

23
Q

pH denatures

A

salt bridges/H-bonding

24
Q

Organic compounds (alcohols) denatures

25
heavy metal ions (Hg, pb, ag ) denature
disulfide bonds
26
mechanical disruption denatures
H-bonding/hydrophobic interactions
27
pyrimidine
six sided double bonded ring with 2 nitrongens
28
purine
one 6 sided, 1 5 sided rings both with 2 nitrongen for a total of 4 nitrogens
29
nonpolar amino acids
contain carbon side chains
30
polar amino aicds
contain OH, SH,or CONH2
31
polar acidic amino aicds
coo
32
primary structure
sequence of amino acids held together by peptide bonds (backbone)
33
secondary structure
folding patterns in backbone between N-H of amide from one part and c=o from carboxylic acid in another part - a helix b sheet
34
tertiary structure
folding of a polypeptide due to interactions between side chains to other sidechains or the environment.
35
quaternary structure
two or more polypeptide chains or subunits
36
fibrous protein
insoluble in water and only have one type of secondary structure
37
globular proteins
soluble polypeptides folded into spherical shapes
38
enzyme action model: lock and key
active site has a rigid nonflexible shape, enzyme binds only substate that exactly fit the active site
39
enzyme action model: induced-fit model
enzyme structure is flexible and adjusts to the shape of the active site
40
Transferases
catalyze the transfer of a functional group between two compounds.
41
Lyases
catalyzes the addition or removal of a group without hydrolysis
42
isomerases
catalyze the rearrangement of atoms within a substrate
43
Ligases
catalyze the joining of two substrates, using ATP
44
increasing enzyme concentration
increases rate of reaction
45
increasing substrate concentration
increases rate of reaction until it saturates and levels out
46
water soluble vitamins
vitamin B, C, H
47
Fat-soluble Bitamins
A,D,E,K
48
RNA (D-ribose)
OH on 2' pentose
49
DNA (2' deoxy-D-riose)
H on 2' pentose
50
Purine
Adenine and Guanine (double N rings)
51
Pyrimidine
Cytosine, thymine, uracil
52
leading strand lead from
5' to 3' towards the replication fork