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BioChemistry > Chapter 4: Protein And Amino Acid Chemistry > Flashcards

Chapter 4: Protein And Amino Acid Chemistry Flashcards

1
Q

What are proteins?

A

Nitrogenous compounds made of amino acids joined by peptide bonds.

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2
Q

How many amino acids enter in the structure of proteins?

A

20 amino acids.
- 19 amino acids.
- 1 Imino acid.

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3
Q

Imino acid

A

Proline

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4
Q

21st amino acid

A

Selenocysteine

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5
Q

Fatty acid general formula

A

R-CH2 (a on the top) - COOH

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6
Q

Amino acid general formula

A

R - CH (a on the top and NH2 on the bottom) - COOH

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7
Q

Where is the peptide bond formed?

A

Between -COOH of 1 amino acid and NH2 of another amino acid by the removal of water.

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8
Q

Classifications of amino acids

A
  1. Chemical
  2. Metabolic
  3. Polarity
  4. Nutritional
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9
Q

Types of amino acids

A

Aliphatic, aromatic, and heterocyclic.

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10
Q

Types of aliphatic amino acids

A

OH hydroxy a, sulfur aa, COOH ( acidic), and NH2 (basic).

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11
Q

Aliphatic amino acids

A

GAVLI
1. Glycine
2. Alanine
Branched chain amino acids:
3. Valine
4. Leucine
5. Isoleucine

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12
Q

OH

A

SHT
1. Serine
2. Homoserine
3. Threonine

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13
Q

Sulfur

A

CCHM
1. Cystine
2. Cysteine
3. Homocysteine
4. Methionine

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14
Q

COOH

A

GAAG
1. Glutamic acid
2. Aspartic
Amide form of acidic amino acids:
3. Asparagine
4. Glutamine

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15
Q

NH2

A

LHHA
1. Lysine
2. Hydroxy Lysine
3. Histidine
4. Arginine

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16
Q

Aromatic

A

TTP
1. Tryptophan
2. Tyrosine
3. Phenyl alanine

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17
Q

Heterocyclic

A

PHHT
1. Tryptophan
2. Histidine
Imino acids:
3. Proline
4. Hydroxyproline

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18
Q

Classification according to polarity

A
  1. Uncharged non polar amino acids
  2. Uncharged polar amino acids
  3. Charged amino acids
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19
Q

Uncharged non polar amino acids

A

GAVLI MPPT
2 aromatic 1 sulfur 1 heterocyclic
1. Glycine
2. Alanine
3. Valine
4. Leucine
5. Isoleucine
6. Phenyl alanine
7. Tryptophan
8. Methionine
9. Proline

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20
Q

Uncharged polar amino acids

A

OH ( main OH 1 aromatic and 1 Imino acid): serine, threonine, tyrosine, hydroxy proline
SH (main sulfur): cysteine
Amide: glutamine and asparagine

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21
Q

Charged amino acids

A

Basic (NH2)( Di amino mono carboxylic): lysine, hydroxy lysine, histidine, arginine.
Acidic ( basic COOH)( mono amino Di carboxylic) : glutamic acids and aspartic acid (aspartate).

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22
Q

Nutritional classification

A

Essential, semi-essential, and non essential amino acids.

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23
Q

Essential

A

Not formed in the body and should be supplied in diet.

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24
Q

Semi essential

A

Formed in the body at a rate enough for an adult but not for growing children.

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25
Q

No essential

A

Can be formed in the body at a rate enough for adult and growing children.

26
Q

Essential amino acids

A

Vital Lymph
1. Valine
2. Isoleucine
3. Threonine
4. Arginine (semi essential)
5. Leucine
6. Lysine
7. Tryptophan
8. Methionine
9. Phenyl alanine
10. Histidine

27
Q

Semiessential

A

Arginine

28
Q

Non essential

A

The rest of the amino acids

29
Q

Proteins of high biological value

A
  1. Contains all essential amino acids.
  2. Easily digested.
30
Q

Proteins of low biological value

A
  1. Deficient 1 of the 9 essential amino acids.
  2. Difficult to be digested.
31
Q

21st amino acid

A

Selenocysteine

32
Q

Amino acids that don’t enter the structure of the protein

A

Homocysteine and homoserine.

33
Q

Metabolic classifications

A
  1. Ketogenic amino acids
  2. Ketogenic and glucogenic amino acids
  3. Glucogenic amino acids
34
Q

Ketogenic amino acids

A

Acetyl CoA and ketone bodies.
1. Lysine
2 Leucine
The two L’s

35
Q

Ketogenic and glucogenic amino acids

A

Both glucose and ketone bodies.
1. Tryptophan
2. Tyrosine
3. Phenylalanine
4. Isloleucine
All aromatic plus half L

36
Q

Glucogenic amino acids

A

Glucose
- Rest of the amino acids.

37
Q

What’s the difference between selenocysteine and cysteine?

A

Selenocysteine is the 21st amino acid. It is like cysteine but has selenium instead of sulfur.

38
Q

Amphoteric properties of amino acids

A

In acidic media they react as bases and carry positive charges. In alkaline media, they act as acids and carry negative charges.

39
Q

Iso Electric Point (IEP)

A

PH at which the amino acids carries both negative and positive charges (Di polar ion or zwitter ion).

40
Q

IEP PH

A

6.02 PH

41
Q

Migration of amino acids at IEP

A

Amino acids can’t migrate in an electric field at IEP.

42
Q

What are the three forms of amino acids according to PH?

A
  1. Acidic media
    NH3+
  2. Zwitter ion
    COO- and NH3+
  3. Alkaline media
    COO-
43
Q

At what PH is the uncharged form of amino acids found?

A

None

44
Q

How is a peptide bond formed

A

By binding the a amino group of one amino acid with a carboxylic group of another amino acid. (By the removal of water).
Binding of 2 amino acids forms a dipeptide, binding of 3 amino acids forms a tripeptide, and so on.

45
Q

Oligopeptides

A

2-10 amino acids

46
Q

Polypeptide

A

11-49 amino acids

47
Q

Protein

A

More than 50 amino acids.

48
Q

How many amino acids enter the structure of proteins?

A

20

49
Q

What are the functions of proteins?

A

Proteins act as:
1. Enzymes and many hormones.
2. Structural proteins (collagen and elastin).
3. Defense mechanism (immunoglobulins “Igs”)
4. Transport (hemoglobin is a carrier of O2).
5. Provide essential amino acids.
6. Plasma proteins (osmotic pressure of the blood)?
7. Cell membrane receptors and transporters.

50
Q

What is important for the function of proteins?

A

The shape (conformation) of a protein.

51
Q

Fibrous protein axial ratio (length/width)

A

More than 10.

52
Q

Globular protein axial ratio (length/width)

A

Less than 10.

53
Q

Fibrous protein structure

A

Arranged around a single axis in a parallel form forming long fibers.

54
Q

Globular protein structure

A

Tightly folded into a compact spherical or globular form.

55
Q

Fibrous protein function

A

Supportive and protective functions.

56
Q

Globular proteins functions

A

Mobile and dynamic functions.

57
Q

Fibrous proteins solubility

A

Insoluble in water.

58
Q

Globular protein solubility

A

Soluble in water.

59
Q

Examples of fibrous proteins

A
  1. Collagen
  2. Elastin
  3. Keratin
60
Q

Globular proteins examples

A
  1. Enzymes
  2. Hormones
  3. Immunoglobulins
  4. Plasma proteins
61
Q

What are the 4 levels of conformation of proteins?

A
  1. Primary structure.
  2. Secondary structure.
  3. Tertiary structure.
  4. Quaternary structure.
62
Q

Primary structure definition

A

Number and sequence of amino acids that forms the backbone of the pol

BioChemistry (8 decks)

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