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Biochemistry > Amino Acids and Peptides > Flashcards

Amino Acids and Peptides Flashcards

1
Q

popular amino acid salt seasoning or food flavor enhancer in many Asian countries especially in East and Southeast Asia

A

monosodium glutamate

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2
Q

Discovered by Japanese chemist Kikunae Ikeda in 1908

A

MSG

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3
Q

Ikeda isolated the compound from food sources and identified it as a basis for this type of taste

A

unani

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4
Q

Fifth basic taste which means rich meaty or savory taste

A

umami

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5
Q

Ikaeda founded this company which mass produced MSG and popularized its use

A

ajinomoto

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6
Q

MSG was widely maligned in the US and was dubbed this

A

chinese restaurant syndrome

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7
Q

Alleged symptoms of headache, flushing, and sweating associated with eating of MSG-laden cuisine in Chinese restaurant

A

chinese restaurant syndrome

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8
Q

amino acid that is naturally abundant in meat products, mushrooms, cheeses, and fermented products

A

glutamate

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9
Q

average person’s intake of glutamate

A

10-20g

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10
Q

receptor where glutamate binds to give food the characteristic savory flavor

A

umami receptor

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11
Q

Major excitatory neurotransmitter in the human brain that plays a key

A

umami receptor

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12
Q

generally regarded as safe for use as seasoning, and its touted neurologic side effects has been debunked because dietary glutamate cannot cross the blood-brain barrier

A

MSG

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13
Q

the real problem with MSG-laden snack foods

A

high salt content

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14
Q

building blocks of protein

A

amino acids

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15
Q

Three structural features in amino acids:

A

➢α-amino group
➢α-carboxylic acid
➢vaiable functional group

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16
Q

form of amino acid where the H+ of the carboxylic acid was donated to the amine

A

zwitterionic form

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17
Q

has an equal number positive and negative charges so its net charge is zero

A

zwitterionic form

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17
Q

located to the left side, hence, the complete designation is L-α-amino acid

A

α-amino group

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18
Q

all standard amino acid are therefore said to be _____handed

A

left handed

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19
Q

the designation of left handedness of amino acid implies this nature of amino
acids which make them capable of rotating plane-polarized light in solution

A

chiral

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20
Q

determines the identity of an amino acid

A

R-group, side chain

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21
Q

nonpolar and neutral amino acids which includes (GAVLI):

A

aliphatic amino acid

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22
Q

pertaining to nonaromatic hydrocarbon compounds in which the constituent carbon atoms can be straight-chain, branched chain, or cyclic, as in alicyclic compounds; saturated, as in the paraffins; or unsaturated, as in the olefins and alkynes

A

aliphatic

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23
Q

example of aliphatic AA

A

Glycine
Alanine
Valine
Leucine
Isoleucine

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24
Q

non-polar and neutral amino acid which has a secondary cyclic amine which is known as imine

A

secondary amine or imino acid

25
Q

example of secondary amine or imino acid

A

proline

26
Q

non-polar and neutral amino acids with bulky aromatic side chain which includes (FYW):

A

aromatic AA

27
Q

example of aromatic AA

A

tyrosine
tryptophan
phenylalanine

28
Q

polar and neutral amino acids with hydroxyl side chain which includes (ST):

A

alcoholic AA

29
Q

example of alcoholic AA

A

serine
threonine

30
Q

slightly polar and neutral amino acids with sulfur-containing side chain which includes (CM

A

sulfur-containing AA

31
Q

example of sulfur containing AA

A

cysteine
methionine

32
Q

polar and negatively charged amino acids with carboxylic acid side chain which includes

A

acidic AA

33
Q

acidic AA

A

glumatic acid
aspartic actid

34
Q

polar and positively charged amino acids with amine side chain (KHR)

A

basic AA

35
Q

example of basic AA

A

Lysine
Arginine
Histidine

36
Q

means that they can behave both as an acid and base

A

amphoteric

37
Q

ionizable group that can accept or donate H+ at a particular pH

A

prototrophic

38
Q

value for the α-COOH group which is expected on the acidic pH range

A

pka1

39
Q

α-NH2 group which is expected on the basic pH range

A

pka2

40
Q

R group in which pH depends on the nature of amino acids

A

pka3

41
Q

most useful way of investigating the acid-base properties of amino acids and peptides

A

titration

42
Q

Involves the progressive neutralization of all prototrophic groups

A

titration

43
Q

titration profile of tryptophan

A

check answer in reviewer

44
Q

shows the change in pH of an amino acid in the process of titration

A

titration curve

45
Q

this value of the prototrophic group can be determined from the titration curve

A

pka

46
Q

point where there is sudden change in the slope of the curve

A

inflection points

47
Q

medial zones of two pKa values where pH change is the slowest

A

buffering region

48
Q

located within the buffering zone of an amino acid

A

pI

49
Q

its pI showed that it is an effective buffer at physiologic pH

A

histidine

50
Q

short amino chain of amino acids which are linked together by amide bond between the α
-carboxylic group of one amino acid can react with the α-amino group of another

A

peptide

51
Q

amine bond that connects the two amino acids

A

peptide bond

52
Q

free amino group

A

n-terminal group

53
Q

free α-carboxylic acid
*
n to c terminal – peptides are always named in this order

A

c-terminal group

54
Q

suffix added to the n-terminal

A

-yl

55
Q

recommended to show the titration process of peptides

A

structural condensation

56
Q

useful way of analyzing the acid-base properties of amino acids and peptides

A

titration

57
Q

➢
Useful way of identifying an unknown amino acid based on its pKa values and pI

A

titration

58
Q

reveals which species predominates at particular pH

A

titrimetric profile

59
Q

recite procedure of amino acid titration

A

EXPERIMENT ON AMINO ACID TITRATION
1.
Weigh 0.25g of unknown amino acid sample in a 250 ml beaker using toploading balance
2.
Add 15ml of distilled water and stir to dissolve the sample
3.
Using a syringe, add 0.200 M HCl while stirring until the pH of the solution drops to 1.50
4.
Titrate with 0.20 ml increments of 0.200 M NaOH, stir then measure the pH after each increment and record the volume of NaOH and pH values
5.
Continue the process until the pH of the solution reaches past 11
6.
Using MS Excel, graph the pH against the volution of the added NaOH
7.
Analyze the resulting titration curve and estimate the pka values from the inflection points of the curve
8.
Determine the unknown amino acid based on the identified experimental pKa values, compare the experimental pka values with the theoretical values and calculate the percent error
9.
Draw the titrimetric profile of the identified amino acid. Calculate the theoretical and experimental pI of the amino acid and determine percent error

60
Q
A

Biochemistry (12 decks)

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