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Dental Biochemistry > Lecture 2 > Flashcards

Lecture 2 Flashcards

1
Q

nuclear proteins

A

RNA, DNA

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2
Q

immunoglobulin example

A

antibody

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3
Q

invader that causes the immune response

A

antigen

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4
Q

proteins are made of

A

amino acids

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5
Q

L amino acid and D amino acid are blank

A

mirror images (stereoisomers)

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6
Q

molecule with both + and - charges

A

zwitterions

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7
Q

molecule that acts as acid base

A

ampholyte

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8
Q

charged ends of amino acids form blank bond

A

peptide

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9
Q

peptide bond aka blank bond

A

amide

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10
Q

two amino acids are joined with the accompanying loss of a water molecule

A

condensation reaction

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11
Q

condensation reaction is catalyzed by the blank

A

ribosome

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12
Q

water inhibits blank

A

protein synthesis

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13
Q

end terminus of peptide chain

A

carboxyl

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14
Q

terminus of peptide chain that is at the beginning

A

amino group

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15
Q

number of R group options…. R groups are amino acids in proteins

A

20

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16
Q

two cysteines can react together to form a strong covalent blank bond

A

disulphide

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17
Q

proteins are purified to be used in

A

drugs

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18
Q

gel electrophoresis distributes and purifies proteins according to blank

A

charge

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19
Q

small proteins migrate blank in gel electrophoresis

A

fast

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20
Q

ion exchange does not usually fully blank proteins

A

purify

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21
Q

size exclusions has blank getting through first

A

large

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22
Q

sds gel electrophoresis separates by size and allows large proteins through blank than smaller

A

slower

23
Q

proton donor

A

acid

24
Q

proton acceptor

A

base

25
Q

strong acids and bases blank in water

A

dissociate completely

26
Q

weak acids make good blank because they dissociate blank in water

A

buffers, incompletely

27
Q

the larger Ka, the blank the tendency for the acid to dissociate

A

greater

28
Q

large Ka means blank acid

A

strong

29
Q

strong acid means a blank pKa

A

small

30
Q

pKa = -(log10) Ka

A

henderson hasselbeck

31
Q

Ka of a weak base is actually a measure of the dissociation a proton from its blank

A

conjugate acid

32
Q

measure of ionizable species in a solution

A

titration curve

33
Q

pH at which the net charge on species is zero on average

A

isoelectric point

34
Q

at blank, 50% protonated 50% unprotonated

A

pKa

35
Q

solution pH higher than the pKa of amino acid, then amino acid is blank

A

deprotonated

36
Q

solution pH lower than the pKa of amino acid, then amino acid is blank

A

protonated (has all its protons)

37
Q

net charge of protein is the blank of all ionic species

A

mean

38
Q

henderson hasselbeck equation

A

pH = pKa + log (products/reactants)

39
Q

a buffer is a weak acid or base and a blank of that weak acid or base

A

salt

40
Q

biological buffers funciton

A

maintain homeostasis

41
Q

2 carriers of oxygen proteins

A

hemoglobin, myoglobin

42
Q

straight or branched CHn chain

A

aliphatic

43
Q

nonpolar small aliphatic aa

A

gly, ala

44
Q

Nonpolar, aliphatic (bulky)

A

VAL, LEU, ILE

45
Q

Branched-chain

A

VAL, ILE, LEU, ARG, ASN, GLN

46
Q

Aromatic

A

PHE, TYR, TRP

47
Q

Charged, acidic (negative)

A

ASP, GLU

48
Q

Charged, basic (positive)

A

HIS, LYS, ARG

49
Q

Polar, uncharged, amides

A

ASN [–> ASP], GLN [–> GLU]

50
Q

Polar, uncharged, hydroxy

A

TRY, SER, THR

51
Q

Polar, uncharged, sulfur-containing

A

MET, CYS

52
Q

only amino acid that is not optically active

A

glycine

53
Q

very hydrophobic aromatics

A

phenylalanine, Tryptophan… not tyrosine because of hydroxyl group

54
Q

blank side chains act as buffers at physiological pH

A

histidine

Dental Biochemistry (43 decks)

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