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_________are compounds in which one or more of the hydrogen atoms of the ammonia molecule have been replaced by hydrocarbon groups.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

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2
Q

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

A

Amines

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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

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4
Q

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

A

Amines

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5
Q

Proteins with only 1 peptide chain. (Tertiary Structure)

A

Monomeric proteins

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6
Q

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

A

Multimeric Proteins

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7
Q

only one kind of polypeptide

A

Homomultimeric

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8
Q

Several different kinds of polypeptide chains

A

Heteromultimeric

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9
Q

Each amino acid in a peptide

A

Moiety or Residue

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10
Q

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

A

N-terminal residue

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11
Q

The residue has a free carboxyl group.

A

C-terminal residue

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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

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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

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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

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15
Q

It depends on the side chain

A

Amino acids

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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

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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

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18
Q

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

A

Ninhydrin Test

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19
Q

Reagent - Ninhydrin Solution

A

Ninhydrin Test

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20
Q

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

A

Ninhydrin Test

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21
Q

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

A

amines

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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

A

20

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

D and L configuration

25
Q

The _______ and _________in aa undergo internal acid-base
reaction to form an internal salt

A

amino and carboxyl groups

26
Q

amino acids can exist as _________ or polar ions:

A

zwitterions

27
Q

It formed by condensation reaction of amino acids with the removal of
water

A

Peptides

28
Q
  • 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
A

Proteins

29
Q
  • 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
A

Proteins

30
Q

It was made up of one or more polypeptides folded in specific conformations

A

Protein

31
Q

_____________ is a linear polymer of amino acids.

A

Polypeptide chain

32
Q

The sequential order of aa along the chain is a characteristic for a given protein. (N-terminal and C-terminal)

A

Primary Structure

33
Q
  • 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
A

Secondary Structure

34
Q
  • 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)
A

Tertiary Structure

35
Q

It describes the organization of subunits in a protein with multiple subunits (oligomeric protein)

A

Quaternary Structure

36
Q
  • 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
A

Protein Denaturation

37
Q
  • 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)
A

Protein Denaturation

38
Q

It is used to detect the presence of two or more peptide linkages in proteins and their larger hydrolytic products (proteoses and peptones).

A

Biuret Test

39
Q

Reagent: alkaline copper (II) sulfate

A

Biuret Test

40
Q

(+) result: formation of violet-colored coordination
complex due to the coordination of cupric ions with
the unshared electron pairs of the peptide

A

Biuret Test

41
Q

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

A

Reaction with Lead Acetate

42
Q

Reagent: NaOH/Pb(CH3 COO)

A

Reaction with Lead Acetate

43
Q

(+) result: Formation of black precipitate

A

Reaction with Lead Acetate

44
Q

____________ 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.

A

Protein Denaturation

45
Q
  • May be caused by the action of heat, light, alcohols,
    strong acids and bases, and other denaturing agents.
A

Protein Denaturation

46
Q

(+) result: appearance of precipitate or coagulated product

A

Protein Denaturation

47
Q

Treatment of amine with benzesulfonyl in aqueous sodium hydroxide and then acidified with HCL

A

Hinsberg Test

48
Q

Addition of Hinsberg Solution in primary amines will results to

A

clear solution (+)

49
Q

Addition of Hinsberg Solution in secondary amines will results to

A

suspension or oil formation (-)

50
Q

Addition of Hinsberg Solution in tertiary amines will results to

A

suspension or oil formation (-)

51
Q

Addition of HCL to 1 amines will results to

A

appearance of precipitate

52
Q

Addition of HCL to 2 amines will results to

A

suspension or oil formation

53
Q

Addition of HCL to 3 amines will results to

A

clear solution