Amines, Amino Acids and Protein Flashcards

1
Q

_________are compounds in which one or more of the hydrogen atoms of the ammonia molecule have been replaced by hydrocarbon groups.

A

Amines

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
2
Q

____________ are classified as 1, 2 or 3 according to the number of hydrogen atoms that have been replaced

A

Amines

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
3
Q
  • the unshared electron pair on the N atom is responsible for most of the chemical properties of amines
  • It act as Lewis bases and are nucleophiles
  • It also make an aromatic ring strongly activated towards electrophilic aromatic substitution (EAS) reactions
A

Amines

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
4
Q

They are polar compounds, and both 1° and 2° amines form
intermolecular hydrogen bond

A

Amines

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
5
Q

Proteins with only 1 peptide chain. (Tertiary Structure)

A

Monomeric proteins

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
6
Q

Proteins with more than 1 polypeptide chain. (Quaternary Peptides)

A

Multimeric Proteins

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
7
Q

only one kind of polypeptide

A

Homomultimeric

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
8
Q

Several different kinds of polypeptide chains

A

Heteromultimeric

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
9
Q

Each amino acid in a peptide

A

Moiety or Residue

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
10
Q

The residue has a free a-amino group. The 1st amino acid in the sequence

A

N-terminal residue

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
11
Q

The residue has a free carboxyl group.

A

C-terminal residue

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
12
Q
  • They are basic compounds
  • Small aliphatic amines (< 5C) are water-soluble and their solutions give a basic response (pH>7) when tested with litmus paper
A

Solubility of Amines in Water

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
13
Q
  • As the number of C atoms increases, solubility decreases
  • Although most amines are not-soluble, amine salts are generally water soluble
A

Solubility of Amines in Water

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
14
Q
  • More substituted or the larger the nonpolar group, the less soluble the sample is.
  • The more substituted, the more basic
A

Solubility of Amines in Water

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
15
Q

It depends on the side chain

A

Amino acids

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
16
Q

Solubility in 6M HCl is a positive identification test for bases. Amines that are insoluble in pure water will be soluble in acid due to the formation of an ammonium chloride salt.

A

Solubility of Amines in Aqueous Acid

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
17
Q

In solubility of Amines in Water, ________ are readily protonated by strong acids such as HCL and H2SO4.
- _______ react with acids forming positively charge quaternary amines

A

Amines

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
18
Q

Generally used to detect the presence of the free a-amino groups in amino acids, polypeptides and proteins

A

Ninhydrin Test

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
19
Q

Reagent - Ninhydrin Solution

A

Ninhydrin Test

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
20
Q

Positive Result: Appearance of blue to violet colored spot due to the formation of diketohydrindamine (DYDA)

A

Ninhydrin Test

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
21
Q

____________, whether soluble or insoluble in water, react quantitatively with
strong acids to form water-soluble salts.

A

amines

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
22
Q

-__________are the building blocks of proteins.
- Each ___________ has a carboxyl group, an amino group, and a
distinctive side chain (R-group) bonded to the ∝-carbon

A

Amino acid

23
Q

there are about ___ different α-amino acids obtained from the hydrolysis of
different proteins and they differ only in the nature of the R groups

24
Q
  • absolute configuration
  • It does not indicate the direction by which the molecule rotate plane
    polarized light
A

D and L configuration

25
The _______ and _________in aa undergo internal acid-base reaction to form an internal salt
amino and carboxyl groups
26
amino acids can exist as _________ or polar ions:
zwitterions
27
It formed by condensation reaction of amino acids with the removal of water
Peptides
28
- They are complex nitrogenous organic substances involved in all phases of cell metabolism - They very large and essentially consist of one or more long chains which are coiled and folded in a definite number
Proteins
29
- Its individual chains are made up of amino acids which are connected by amide linkages or peptide bonds. - Hydrolysis of proteins yields the component amino acids
Proteins
30
It was made up of one or more polypeptides folded in specific conformations
Protein
31
_____________ is a linear polymer of amino acids.
Polypeptide chain
32
The sequential order of aa along the chain is a characteristic for a given protein. (N-terminal and C-terminal)
Primary Structure
33
- refers to the manner in which the aa are arranged in space - some protein chains are arranged in the form of α-helix or β-pleated sheet
Secondary Structure
34
- It refers to the manner in which the protein molecule is folded - polypeptide chains arranged in long strands or sheets (fibrous) - polypeptide chains folded into spherical or globular shape (globular)
Tertiary Structure
35
It describes the organization of subunits in a protein with multiple subunits (oligomeric protein)
Quaternary Structure
36
- the biological activity of a protein depends on its structure - destruction of protein’s proper conformation - disruption of forces that stabilize the 2, 3 and 4 structures
Protein Denaturation
37
- Results in changes in physical properties (precipitation or coagulation) and loss of biological activity - It may be caused by the action of heat, light, and chemical agents such as alcohols, strong acids and bases, detergents, and heavy metals such as Hg (II) and Pb (II)
Protein Denaturation
38
It is used to detect the presence of two or more peptide linkages in proteins and their larger hydrolytic products (proteoses and peptones).
Biuret Test
39
Reagent: alkaline copper (II) sulfate
Biuret Test
40
(+) result: formation of violet-colored coordination complex due to the coordination of cupric ions with the unshared electron pairs of the peptide
Biuret Test
41
Sulfur in sulfur-containing proteins and amino acids can be released as sulfides by the action of strong alkali. - the sulfides can be precipitated by lead acetate
Reaction with Lead Acetate
42
Reagent: NaOH/Pb(CH3 COO)
Reaction with Lead Acetate
43
(+) result: Formation of black precipitate
Reaction with Lead Acetate
44
____________ is associated with the alteration of the secondary and tertiary structures of biological proteins which results in changes in physical properties and loss of biological activity.
Protein Denaturation
45
- May be caused by the action of heat, light, alcohols, strong acids and bases, and other denaturing agents.
Protein Denaturation
46
(+) result: appearance of precipitate or coagulated product
Protein Denaturation
47
Treatment of amine with benzesulfonyl in aqueous sodium hydroxide and then acidified with HCL
Hinsberg Test
48
Addition of Hinsberg Solution in primary amines will results to
clear solution (+)
49
Addition of Hinsberg Solution in secondary amines will results to
suspension or oil formation (-)
50
Addition of Hinsberg Solution in tertiary amines will results to
suspension or oil formation (-)
51
Addition of HCL to 1 amines will results to
appearance of precipitate
52
Addition of HCL to 2 amines will results to
suspension or oil formation
53
Addition of HCL to 3 amines will results to
clear solution