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BIOCHEM LEC > MOD 2 L1 > Flashcards

MOD 2 L1 Flashcards

1
Q

general formula for amino acids

A

amino group - c (with side chain sa baba) - carboxylic acid

NH - C - COOH

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2
Q

most ABUNDANT & FUNCTIONALLY DIVERSE molecules in living systems

A

PROTEINS

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3
Q

it is a LARGE MOLECULE that contains carbon, hydrogen, oxygen, & nitrogen (CHON)

A

PROTEINS

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4
Q

the chiral carbon is also called as

A

α - carbon (alpha carbon)

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5
Q

has 4 different groups attached to it

A

CHIRAL CENTER

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6
Q

what forms a peptide bond in amino acids

A

AMINO GROUP & CARBOXYLIC ACID GROUP

NH & COOH

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7
Q

proteins are

A

POLYPEPTIDE

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8
Q

every function in the living cells are HIGHLY DEPENDENT on

A

PROTEINS

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9
Q

a specialized protein of FLAGELLA is called

A

FLAGELLIN

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10
Q

an example of GLOBULAR PROTEIN

A

HEMOGLOBIN

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11
Q

component of hemoglobin that is RESPONSIBLE FOR THE PIGMENT or the red color of our blood

A

HEME

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12
Q

hemoglobin is a

A

TETRAMERIC

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13
Q

sides / groups of hemoglobin

A

2 - α
2- β

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14
Q

a special nucleus found in hemoglobin is known as

A

PROTOPHORPYRIN

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15
Q

turn genes ON & OFF to guide the differentiation of the cell and its later responsiveness to signals reaching it

A

TRANSCRIPTION FACTORS

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16
Q

the PRIMARY FUNCTION of protein is to provide the needed amino acids for maintaining an

A

ANABOLIC STATE

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17
Q

proteins play a vital role in the ________ system

A

NEURO-ENDOCRINE

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18
Q

one of the by product of protein metabolism

A

UREA

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19
Q

how many amino acids are involved in TRANSLATION

A

20

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20
Q

protein synthesis

A

TRANSLATION

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21
Q

how many amino acids are PRODUCED BY HUMANS?

A

AT LEAST 10

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22
Q

saan manggagaling ung another 10 amino acids that our body cannot produce

A

they must be supplemented in our diet

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23
Q

the other 10 amino acids that our body CANNOT PRODUCE is referred to as

A

ESSENTIAL AMINO ACIDS

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24
Q

what type of amino acids are produced by humans

A

L - α

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25
Q

what type of amino acids are produced by microorganisms

A

D amino acids

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26
Q

predominant amino acid in BACILLUS SUBTILIS

A

D-METHIONINE

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27
Q

Bacitracin & Gramicidin A

A

ANTIBIOTICS

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28
Q

Bleomycin

A

ANTITUMOR AGENT

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29
Q

Microcystin & Nodularin

A

CYANOBACTERIAL PEPTIDES

30
Q

metabolic product of bacillus subtilis

A

BACITRACIN

31
Q

has TYROCIDIN

A

GRAMICIDIN A

32
Q

common side effect of BLEOMYCIN

A

pulmonary fibrosis

33
Q

toxic microbial peptides

A

CYANOBACTERIAL PEPTIDES

34
Q

an IMINO ACID

A

PROLINE

35
Q

all amino acids posses the same functional group except

A

PROLINE

36
Q

formed by the COOH of an amino acid and the NH₂ of the next amino acid

A

PEPTIDE BOND

37
Q

peptide bonds has the capability to rotate because of this characteristic

A

PARTIAL DOUBLE BOND

38
Q

the protation of peptide bonds are termed as

A

RESONANCE

39
Q

forms a typical peptide group

A

RESONANCE

40
Q

uncharged, single-bonded form is typically

A

60%

41
Q

charged, double-bonded form is typically

A

40%

42
Q

the peptide bond is an __ bond

A

AMINE BOND

43
Q

these are very STABLE and NEUTRAL

A

AMIDES

44
Q

amino acids are linked by

A

PEPTIDE BONDS

45
Q

naming of peptides

A

drop -ine, palitan ng -yl
retained ang name ng terminal amino acid ( yung nasa dulo)

46
Q

useful in classifying amino acids

A

R GROUP

47
Q

the genetic code specifies how many amino acids

A

20

48
Q

only what amino acids in human occurs in proteins

A

L - α amino acids

49
Q

represents the vast majority of amino acids found in proteins

A

L-amino acids

50
Q

found in some antibiotics and in the bacterial cell wall

A

D-amino acids

51
Q

REACTIONS OF AMINO ACIDS

responsible for:
* acylation
* amidation
* esterification

A

AMINE GROUP

52
Q

REACTIONS OF AMINO ACIDS

responsible for:
* esterification
* formation of amides and acid anhydrides

A

CARBOXYLIC ACID GROUP

53
Q

the most important reaction of amno acids

A

PEPTIDE BOND FORMATION

54
Q
  • tend to interact with the aqueous environment, often involved in the formation of H-bonds
  • predominnatly found on the exterior surfaces of proteins or in the reactive centers of enzymes
  • Ser, Thr, Tyr
A

HYDROPHILIC AMINO ACIDS

55
Q
  • tend to repel the aqueous environment
  • do not ionize or participate in the formation of H-bonds
  • reside predominantly in the interior of proteins
  • Ala, Val, Leu, Ile
A

HYDROPHOBIC AMINO ACIDS

56
Q

allow enzyme reactions to occur

A

R GROUPS

57
Q

act as either a proton donor or acceptor at physiological pH, thus play a important role in enzymatic catalysis

A

IMIDAZOLE RING og [H]

58
Q

allow serine and threonine, cysteine to act as nucleophiles during enzymatic catalysis

A

primary alcohol of ser & thr
thiol of cys

59
Q

____ of cysteine able to form a disulfide bonds with other cysteines

A

THIOL

60
Q

____ of ser, tyr, and thr participate in the regulation of activity of enzymes

A

OH GROUP

61
Q

amino aids may have positive, negative, or zero net charge

A

ZWITTERIONS

62
Q

charge of zwitterion

A

both + & - charge

63
Q

zwitterion is ____ overall

A

neutral

64
Q

TESTS

  • used to visualize spots or bands of amino acids separated by chromatography or electrophoresis
  • deep purple color is formed with traces of any amino acid
  • RUHEMANN’S PURPLE
A

REACTION W/ NINHYDRIN

65
Q

TESTS

  • General test for the presence of protein
  • turns purple when mixed with a solution containing protein
  • purple color is formed when copper ions in the reagent react with the peptide bonds of the polypeptide chains to form a complex
A

BIURET TEST

66
Q

requirement of biuret test

A

should be polypeptide

kapag tripeptide, negative ang result

67
Q

TESTS

  • used to determine the presence of aromatic amino acids
  • concentrated nitric acid will form a yellow complex with tryptophan and tyrosine side chains in proteins
A

XANTHOPROTEIC TEST

68
Q

TESTS

test for tyrosine

A

MILLON’S TEST

69
Q

TESTS

test for tryptophan

A

HOPKIN’S

70
Q

TESTS

  • disulfide bridges wil react with Pb²+ ion from lead acetate in an acidified solution
  • a black precipitate (PbS) indicates the presence of disulfide bonded cysteine in proteins
A

LEAD ACETATE TEST

BIOCHEM LEC (29 decks)

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