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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
No essential
Can be formed in the body at a rate enough for adult and growing children.
26
Essential amino acids
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
Semiessential
Arginine
28
Non essential
The rest of the amino acids
29
Proteins of high biological value
1. Contains all essential amino acids. 2. Easily digested.
30
Proteins of low biological value
1. Deficient 1 of the 9 essential amino acids. 2. Difficult to be digested.
31
21st amino acid
Selenocysteine
32
Amino acids that don’t enter the structure of the protein
Homocysteine and homoserine.
33
Metabolic classifications
1. Ketogenic amino acids 2. Ketogenic and glucogenic amino acids 3. Glucogenic amino acids
34
Ketogenic amino acids
Acetyl CoA and ketone bodies. 1. Lysine 2 Leucine The two L’s
35
Ketogenic and glucogenic amino acids
Both glucose and ketone bodies. 1. Tryptophan 2. Tyrosine 3. Phenylalanine 4. Isloleucine All aromatic plus half L
36
Glucogenic amino acids
Glucose - Rest of the amino acids.
37
What’s the difference between selenocysteine and cysteine?
Selenocysteine is the 21st amino acid. It is like cysteine but has selenium instead of sulfur.
38
Amphoteric properties of amino acids
In acidic media they react as bases and carry positive charges. In alkaline media, they act as acids and carry negative charges.
39
Iso Electric Point (IEP)
PH at which the amino acids carries both negative and positive charges (Di polar ion or zwitter ion).
40
IEP PH
6.02 PH
41
Migration of amino acids at IEP
Amino acids can’t migrate in an electric field at IEP.
42
What are the three forms of amino acids according to PH?
1. Acidic media NH3+ 2. Zwitter ion COO- and NH3+ 3. Alkaline media COO-
43
At what PH is the uncharged form of amino acids found?
None
44
How is a peptide bond formed
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
Oligopeptides
2-10 amino acids
46
Polypeptide
11-49 amino acids
47
Protein
More than 50 amino acids.
48
How many amino acids enter the structure of proteins?
20
49
What are the functions of proteins?
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
What is important for the function of proteins?
The shape (conformation) of a protein.
51
Fibrous protein axial ratio (length/width)
More than 10.
52
Globular protein axial ratio (length/width)
Less than 10.
53
Fibrous protein structure
Arranged around a single axis in a parallel form forming long fibers.
54
Globular protein structure
Tightly folded into a compact spherical or globular form.
55
Fibrous protein function
Supportive and protective functions.
56
Globular proteins functions
Mobile and dynamic functions.
57
Fibrous proteins solubility
Insoluble in water.
58
Globular protein solubility
Soluble in water.
59
Examples of fibrous proteins
1. Collagen 2. Elastin 3. Keratin
60
Globular proteins examples
1. Enzymes 2. Hormones 3. Immunoglobulins 4. Plasma proteins
61
What are the 4 levels of conformation of proteins?
1. Primary structure. 2. Secondary structure. 3. Tertiary structure. 4. Quaternary structure.
62
Primary structure definition
Number and sequence of amino acids that forms the backbone of the pol

BioChemistry (8 decks)

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