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Biology, Chemestry > chem exam 3 > Flashcards

chem exam 3 Flashcards

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AP® Biology flashcards Biology 101 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

A

H-bonding

25
Q

heavy metal ions (Hg, pb, ag ) denature

A

disulfide bonds

26
Q

mechanical disruption denatures

A

H-bonding/hydrophobic interactions

27
Q

pyrimidine

A

six sided double bonded ring with 2 nitrongens

28
Q

purine

A

one 6 sided, 1 5 sided rings both with 2 nitrongen for a total of 4 nitrogens

29
Q

nonpolar amino acids

A

contain carbon side chains

30
Q

polar amino aicds

A

contain OH, SH,or CONH2

31
Q

polar acidic amino aicds

A

coo

32
Q

primary structure

A

sequence of amino acids held together by peptide bonds (backbone)

33
Q

secondary structure

A

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
Q

tertiary structure

A

folding of a polypeptide due to interactions between side chains to other sidechains or the environment.

35
Q

quaternary structure

A

two or more polypeptide chains or subunits

36
Q

fibrous protein

A

insoluble in water and only have one type of secondary structure

37
Q

globular proteins

A

soluble polypeptides folded into spherical shapes

38
Q

enzyme action model: lock and key

A

active site has a rigid nonflexible shape, enzyme binds only substate that exactly fit the active site

39
Q

enzyme action model: induced-fit model

A

enzyme structure is flexible and adjusts to the shape of the active site

40
Q

Transferases

A

catalyze the transfer of a functional group between two compounds.

41
Q

Lyases

A

catalyzes the addition or removal of a group without hydrolysis

42
Q

isomerases

A

catalyze the rearrangement of atoms within a substrate

43
Q

Ligases

A

catalyze the joining of two substrates, using ATP

44
Q

increasing enzyme concentration

A

increases rate of reaction

45
Q

increasing substrate concentration

A

increases rate of reaction until it saturates and levels out

46
Q

water soluble vitamins

A

vitamin B, C, H

47
Q

Fat-soluble Bitamins

A

A,D,E,K

48
Q

RNA (D-ribose)

A

OH on 2’ pentose

49
Q

DNA (2’ deoxy-D-riose)

A

H on 2’ pentose

50
Q

Purine

A

Adenine and Guanine (double N rings)

51
Q

Pyrimidine

A

Cytosine, thymine, uracil

52
Q

leading strand lead from

A

5’ to 3’ towards the replication fork

Biology, Chemestry (10 decks)

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