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
Tyrosine is essential A.A. | T or F
F non essential
26
Ketogenic amino acid....
Leucine
27
Mixed A.A (ketogenic and glucogenic )....
``` Tyrosine Treptophan Phenylalanine Lysine Isoleucine ```
28
The amino group is attached to the alpha carbon next to the carboxyl group except.....
Proline
29
The alpha carbon in all amino acids are asymmetric except ......
Glycine
30
All amino acids are optrcally active except .....
Glycine
31
All amino acids are L-amino acids what is that mean?
That mean they having their NH2 groups towards the laft
32
The amino acids are amphoteric | T or F
T
33
The PH at which the amino acid carries no net charge is knowing as ......
Isoelectric point
34
Amino acids act as neurotransmitters .....
Glycin | Glutamate
35
A.A used in detoxification
Glycine
36
It is the bond between the hydrogen of -NH group of one amino acid residues and the carbonyl oxygen of the furth one
Hydrogen bond in 2ry protein structure
37
Types of protein fold 2ry structure
Alpha helix structure | B-pleated sheet
38
Keratins have ........... structure
Alpha helix structure
39
Is not geometrically compatible with the right-handed spiral of the alpha helix
Imino acid ( proline)
40
If present in large amount can distrupt the alpha helix by forming ionic bonds, or by electrostatically repelling each other
Charged amino acids (Glutamate,Aspartate, Histidine, Lysine, Arginine) مجموعين بكلمة (GAHLA) جاهلة 🤣🤣
41
Bulky side chain A.A distrupt the alpha helix
Tryptophan
42
Amino acids branched at the B-carbon and distrupt the alpha helix
Valine and isoleucine
43
Is formed between tow or more separated polypeptide chains
B-pleated sheet
44
Types of B-pleated sheet
Parallel B-sheet | Antiparallel
45
Polypeptide chains run in the same direction
Parallel B-sheet
46
Polypeptide chains run in the opposite direction
Antiparallel pleated sheet.
47
Permits the change of direction of the peptide chain to get folded structure
Beta bends
48
Gives protein globularity rather than linearity
Beta bends
49
Are found in beta bend
Proline and glycine
50
Is folding pattern of the secondary structural elements into the fibal three fimentional conformation
3ry structure
51
What are the interaction that stabilizing the 3ry structure?
Hydrophobic bound Disulfide bonds Hydrogen bonds Salts bonds
52
Is the fundamental functional and three-dimensional structure units of polypeptides.
Domine
53
Subunits are held together by non-covalent bonds such as H-bond, ionic bonds, and hydrophobic bonds
Quaternary structure
54
LDH enzyme and Globulin are .....
Quaternary structure
55
What are the effect of protein denaturation?
Loss ofvbiological function | Denaturated proteins are often insoluble and easily precipitated.
56
Causes coagulation and precipitation of certain protien such as albumin.
Heat
57
Interfere with hydrophobic bonds of proteins
Organic solvents and detergents
58
Diseases developed from misfolded protein
Alzaheimer's and Parkinson's disease
59
Albumin and globulin are
Simple protein
60
Globins and protamins are acidic proteins | T or F
F are basic proteins
61
Keratins and collagens and elastin are scleroproteins | T or F
T
62
Gliadins and glutelins are an examples on ...
Acidic proteins
63
Give an examples on conjugated phosphoproteins
Casein (milk protein) | Phosphoenzymes
64
Plasma lipoproteins and cell membrane are ....
Conjugated proteins ( lipoproteins)
65
Hormons (TSH' LH FSH) are....
Conjugated glycoproteins
66
Cell membran are ....
Conjugated proteins (proteoglycan)
67
Chromosomes and RNA are
Nucleoproteins
68
Metaloproteins containing Iron:
Tranferrin Hemoglobin Ferritin
69
Metaloproteins containing copper:
Ceruloplasmin
70
Metaloproteins containing zinc:
Insullin hormone
71
Metaloproteins containing magnesium:
Enzymes like : Kinase, phosphatase
72
Metaloproteins containing selenium
Glutathione perxidase
73
An examples on fibrous proteins.....
Collagen, myosin, keratin
74
An examples on globular proteins ....
Enzymes, insulin, albumin, globulin.