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A.A Flashcards

1
Q

Classification of A.A

A

Chemical
Nutritional
Metabolic

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2
Q

Glycine is …

A

Aliphatic A.A

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3
Q

Alanine is

A

Aliphatic A.A

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4
Q

Valine is …..

A

Aliphatic A.A

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5
Q

Serine is ….

A

Hydroxyl containing aliphatic A.A

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6
Q

Threonine is…

A

Hydroxyl containing amino A.

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7
Q

Cyteine is…..

A

Aliphatic A.A

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8
Q

Cystine is ……

A

Aliphatic A.A

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9
Q

Methionine is …..

A

Aliphatic A.A

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10
Q

What are the sulfur containing A.A?

A

Cysteine
Cystine
Methionine

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11
Q

What are the hydroxyl containing A.A?

A

Threonine
Serine
Tyrosine (aromatic)

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12
Q

What are the branched chain A.A?

A

Valine
Leucine
Isoleucine

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13
Q

Acidic side chain A.A are ….

A

Aspartate

Glutamate

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14
Q

Amidic side chain A.A are …..

A

Asparagine

Glutamine

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15
Q

Aliphatic basic A.A are ……

A

Lysine

Arginine

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16
Q

Aromatic basic A.A is….

A

Histidine

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17
Q

What are the aromatic A.A.?

A

Phenylalanine
Tyrosine (hydroxyl-containing)
Tryptophan
Histidine (basic)

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18
Q

Porline is ….

A

Imino acid

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19
Q

Non polar A.A are …..

A 
Glycine 
Alanine
Valine
Leucine
Isoleucine
Methionine
Proline
Phenylalanine
Treptophan
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20
Q

Uncharged polar A.A are ……..

A 
Serine
Asparagine
Glutamine
Threonine
Tyrosine
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21
Q

What are the essential A.A?

A 
Valine 
Leucine
Isoleucine
Tryptophan
Phenylalanine
Threonine
Methionine
Lysine
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22
Q

Semi essential A.A are …..

A

Arginine

Histidine

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23
Q

Glycine is essential or not essential?

A

Not essential A.A

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24
Q

Alanine is essential A.A

True or f

A

F non essential A.A.

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25
Q

Tyrosine is essential A.A.

T or F

A

F non essential

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26
Q

Ketogenic amino acid….

A

Leucine

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27
Q

Mixed A.A (ketogenic and glucogenic )….

A 
Tyrosine 
Treptophan
Phenylalanine
Lysine
Isoleucine
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28
Q

The amino group is attached to the alpha carbon next to the carboxyl group except…..

A

Proline

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29
Q

The alpha carbon in all amino acids are asymmetric except ……

A

Glycine

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30
Q

All amino acids are optrcally active except …..

31
Q

All amino acids are L-amino acids what is that mean?

A

That mean they having their NH2 groups towards the laft

32
Q

The amino acids are amphoteric

T or F

33
Q

The PH at which the amino acid carries no net charge is knowing as ……

A

Isoelectric point

34
Q

Amino acids act as neurotransmitters …..

A

Glycin

Glutamate

35
Q

A.A used in detoxification

36
Q

It is the bond between the hydrogen of -NH group of one amino acid residues and the carbonyl oxygen of the furth one

A

Hydrogen bond in 2ry protein structure

37
Q

Types of protein fold 2ry structure

A

Alpha helix structure

B-pleated sheet

38
Q

Keratins have ……….. structure

A

Alpha helix structure

39
Q

Is not geometrically compatible with the right-handed spiral of the alpha helix

A

Imino acid ( proline)

40
Q

If present in large amount can distrupt the alpha helix by forming ionic bonds, or by electrostatically repelling each other

A

Charged amino acids (Glutamate,Aspartate, Histidine, Lysine, Arginine)
مجموعين بكلمة (GAHLA) جاهلة 🤣🤣

41
Q

Bulky side chain A.A distrupt the alpha helix

A

Tryptophan

42
Q

Amino acids branched at the B-carbon and distrupt the alpha helix

A

Valine and isoleucine

43
Q

Is formed between tow or more separated polypeptide chains

A

B-pleated sheet

44
Q

Types of B-pleated sheet

A

Parallel B-sheet

Antiparallel

45
Q

Polypeptide chains run in the same direction

A

Parallel B-sheet

46
Q

Polypeptide chains run in the opposite direction

A

Antiparallel pleated sheet.

47
Q

Permits the change of direction of the peptide chain to get folded structure

A

Beta bends

48
Q

Gives protein globularity rather than linearity

A

Beta bends

49
Q

Are found in beta bend

A

Proline and glycine

50
Q

Is folding pattern of the secondary structural elements into the fibal three fimentional conformation

A

3ry structure

51
Q

What are the interaction that stabilizing the 3ry structure?

A

Hydrophobic bound
Disulfide bonds
Hydrogen bonds
Salts bonds

52
Q

Is the fundamental functional and three-dimensional structure units of polypeptides.

53
Q

Subunits are held together by non-covalent bonds such as H-bond, ionic bonds, and hydrophobic bonds

A

Quaternary structure

54
Q

LDH enzyme and Globulin are …..

A

Quaternary structure

55
Q

What are the effect of protein denaturation?

A

Loss ofvbiological function

Denaturated proteins are often insoluble and easily precipitated.

56
Q

Causes coagulation and precipitation of certain protien such as albumin.

57
Q

Interfere with hydrophobic bonds of proteins

A

Organic solvents and detergents

58
Q

Diseases developed from misfolded protein

A

Alzaheimer’s and Parkinson’s disease

59
Q

Albumin and globulin are

A

Simple protein

60
Q

Globins and protamins are acidic proteins

T or F

A

F are basic proteins

61
Q

Keratins and collagens and elastin are scleroproteins

T or F

62
Q

Gliadins and glutelins are an examples on …

A

Acidic proteins

63
Q

Give an examples on conjugated phosphoproteins

A

Casein (milk protein)

Phosphoenzymes

64
Q

Plasma lipoproteins and cell membrane are ….

A

Conjugated proteins ( lipoproteins)

65
Q

Hormons (TSH’ LH FSH) are….

A

Conjugated glycoproteins

66
Q

Cell membran are ….

A

Conjugated proteins (proteoglycan)

67
Q

Chromosomes and RNA are

A

Nucleoproteins

68
Q

Metaloproteins containing Iron:

A

Tranferrin
Hemoglobin
Ferritin

69
Q

Metaloproteins containing copper:

A

Ceruloplasmin

70
Q

Metaloproteins containing zinc:

A

Insullin hormone

71
Q

Metaloproteins containing magnesium:

A

Enzymes like : Kinase, phosphatase

72
Q

Metaloproteins containing selenium

A

Glutathione perxidase

73
Q

An examples on fibrous proteins…..

A

Collagen, myosin, keratin

74
Q

An examples on globular proteins ….

A

Enzymes, insulin, albumin, globulin.

Biochemistry (2 decks)

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