Proteins Flashcards

1
Q

Define proteins and how many functional groups does it contain

A

Molecules composed of 2 functional group
1 amine
2. Carboxyl

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2
Q

Are proteins acids or bases

A

They are acid and bases both at the same time

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3
Q

Define Zwitterions

A

Neutral charged amine acids ions
; at certain isoelectric point positive charges no. Is equal to negative charges no.

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4
Q

What’s the positive and negative charge in the amino acid

A

Positive is the protonated amine group .
Negative is the deprotonated carboxyl group .

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5
Q

Total no. Of amino acids in humans is

A

20

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6
Q

Essential amino acid no

A

10

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7
Q

Mention the 10 essential amino acids

A

Lysine
Methionine
Phenylalanine
Leucine
Isoleucine
Tryptophan
Threonine
Arginine
Histidine
Valine .

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8
Q

Which amino acids that are not strictly essential but depends on age and health status

A

Arginine
Histidine

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9
Q

Mention the amino acids under th 3 As subclasses

A

Acidic GA ; glutamate , aspartate
Aromatic. TpT , tryptophan. Phenylalanine, tyrosine
Alphatic : vagiL valine , alanine , isoleucine , leucine , glycine

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10
Q

Mention amino acid under the basic subclass of the amino acids

A

AHL el basic
Arginine
Histidine
Lysin

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11
Q

Mention the amino acids under the Sulphydryl subclass

A

CM
Cysteine
Methionine

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12
Q

Imino group

A

Proline

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13
Q

Hydroxyl group

A

ST
Therionine
Serine

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14
Q

Which amino acid is the precursor for dopamine and noreadrenaline

A

Tyrosine > L-dopa .

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15
Q

Which precursor for serotonins

A

Tryptophan

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16
Q

Which one is precursor for nitric oxide

A

Arginine

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17
Q

Which amino acid is precursor for porphyrins

A

Glycine

What is the definition of porphyrin?
: any of various compounds with a macrocyclic structure that consists essentially of four pyrrole rings joined by four =CH− groups. especially : one (such as chlorophyll or hemoglobin) containing a central metal atom and usually exhibiting biological activity.

The most common examples are the hemes (found in hemoglobins, myoglobins, cytochromes, catalases, and peroxidases), chlorophylls, and bacteriochlorophylls. Iron is the chelating metal found in hemes,1 and magnesium is found in the numerous chlorophylls and bacteriochlorophylls.

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18
Q

When does detoxification occur

A

It occurs BEFORE urea cycle .

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19
Q

What’s the equation for detoxification

A

Amino acids > glutamic acid > carbamyl phosphate .

20
Q

Where does urea cycle occurs

A

In the liver
Part1 at the liver mitochondria .
Part 2 at the liver cystosol.

21
Q

What car results from amino acid degradation

A

Urea , Uric acid , ammonia .

22
Q

Urea cycle in the liver mitochondria starts with CO

A

Carbamyl phosphate + ornithine
Co

23
Q

Urea cycle in the mitochondria ends with 2As

A

Arginosuccinate + aspartate

24
Q

Mid compound of the urea cycle in the mitochondria is

A

Citruline
ست رول

25
Urea cycle in the cytoplasm
Arginosuccinate > arginine > urea + ornithine
26
What’s the end product of urea cycle in the liver cytoplasm
Urea + ornithine UO
27
What are proteins made of
Proteins are made of polymerized amino acids
28
Which structure binds the polymer chain of the amino acid in the protein
Peptide bonds .
29
Protein structures has 4 distinct aspects
Primary Secondary Tertiary Quaternary
30
Proteins are divided into 3 groups mention
Globular proteins Fibrous protein Membrane proteins
31
Which group of protein will make enzymes and mostly itd]s soluble
Globular proteins
32
Which group of proteins that will form receptors
Membrane proteins
33
Which group of proteins often structural
Fibrous
34
Which structure of protein have peptide bonds
Primary
35
Which structure have disulphide bonds
Tertiary
36
Which protein structure is held by hydrogen bond
Secondary .
37
With structure Is the amino acid sequence
Primary
38
3d form of the primary structure is
2ndry
39
Overall shape of a single molecule protein is
Tertiary
40
Which one controls the basic function of the protein
Tertiary structure
41
Which one forms the arrangement of multiple folds of proteins
Quaternary
42
Define primary structure protein
Amino acid sequence held by peptide bonds
43
Define secondary structure protein
3D form of the primary structure protein Held by hydrogen bonds
44
Define tertiary structure protein
Gives the basic function of the protein held by disulphide bonds And it’s the overall shape of a SINGLE protein molecule.
45
Define the quaternary structure protein>
Is the arrangement of multiple folded protein molecules .