Amino Acids And Proteins Flashcards

1
Q

What is an amino acid

A

A compound whose molecules contain bird an amino and a carboxyl group

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2
Q

How many amino acids occur naturally and in what form

A

20 occur naturally and they combine to form proteins

All naturally occurring amino acids are a amino acids

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3
Q

What does alpha amino acid mean

A

NH2 and COOH are bonded to same C atom

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4
Q

What is the definition of a zwitterion

A

Ions which have a permanent positive and negative charge but which are neutral overall

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5
Q

Why do amino acids exist as zwitterions

A
  • they all contain a basic group and an acidic carboxyl group
  • undergo internal acid-base reaction
  • forms a dipolar ion
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6
Q

Draw the diagram of a zwitterion amino acid

A

See page 22

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7
Q

State the physical properties of amino acids

A

⭕️ High mp - dipolar ions - strong forces of attraction - lot of energy
⭕️ water soluble - dipolar ions - interact w polar water molecules
⭕️ white crystalline solids
⭕️ insoluble in organic solvents

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8
Q

What group is involved in the reaction when an amino acid reacts with sodium carbonate

A

The COOH group

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9
Q

What are the products for the reaction of an amino acid with sodium carbonate

A

Metal salt
Water
Carbon dioxide

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10
Q

What are he observations for amino acid reaction with sodium carbonate

A

Bubbles of colourless has evolved

Solid disappears

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11
Q

What group is reacted when amino acids react with nitrous acid

A

The NH2 group is replaced by an OH

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12
Q

What are the products when amino acid is reacted with nitrous acid

A

N2
H2O
Hydroxycarboxylic acid

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13
Q

How is nitrous acid produced

A

In situ
NaNO2 and HCl
Below 5°C

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14
Q

What is formed when amino acids react with copper (II) sulfate

A

A complex

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15
Q

What are the observations when amino acid is reacted with nitrous acid

A

Bubbles of colourless has given off (N2)

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16
Q

What are the observations when amino acid reacts with copper (II) sulfate

A

Dark blue solution formed

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17
Q

Write the structural equation of amino acid reaction with copper (II) sulfate

A

See notes

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18
Q

Draw the structure of an amino acid in acid conditions and alkaline conditions

A

See notes

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19
Q

Describe the structure of a neutral amino acid

A

Contains one amine and one carboxyl group

20
Q

Describe an acidic amino acid

A

Contains additional carboxyl group

21
Q

Describe a basic amino acid

A

Contains additional amine group

22
Q

What kind of reaction forms a peptide (polyamide)

A

Condensation polymerisation of amino acids

23
Q

What is a peptide link

A

Link between -NH2 of one amino acid and -COOH of another

24
Q

What is a condensation reaction

A

When two molecules combine to form one single molecule. Resulting in the loss of a small molecule eg water

25
Draw the peptide group
See notes
26
What happens during acid hydrolysis of protein
- acids formed are protonated - NH2 ➡️ NH3+ - positive amino acid ions - COOH stays same
27
What happens during alkaline hydrolysis of a proteins
- acids formed are deprotonated - COOH ➡️ COO- - negative amino acid ions - NH2 stays the same
28
What is the definition of primary structure of proteins
Sequence of amino acids joined by peptide links in the chain
29
What is the definition of secondary structure
Twisting/coiling of the chain to form a B-pleated sheet/a helix by intramolecular hydrogen bonding
30
Between which parts of the molecule does H bonding occur in the secondary structure
NH and C=O
31
What is the definition of tertiary structure in proteins
Bending / folding of secondary structure to give a precise 3D shape held together by Hydrogen bonding / disulphide bridges / ionic interactions / VDW forces
32
How does the tertiary structure occur
Interactions between R-group side chains
33
How to sulfer bridges form
- cystine | - side group of SH ➡️ oxidised to form dimer
34
What type of bond is a sulfer bridge
Covalent - stronger than H bond
35
How do ionic interactions occur in tertiary structure
Ionic bonds between adjacent acidic and basic amino acids
36
How do VDW forces occur in tertiary structure
Between non polar side groups
37
How do dipole dipole interactions occur in tertiary structure
Between polar side chains
38
How do hydrophobic interactions occur in tertiary structure
- Between non polar side chains and water - repel water - chain folds and hydrophobic on inside folds and hydrophilic polar groups on outside
39
What is the definition of an enzyme
A protein which is a biological catalyst
40
What do enzymes do
- Speed up reaction without being used up | - alternative reaction pathway of lower activation energy
41
What is the definition of active site
Site on surface of enzyme into which the substrate fits
42
What is the induced fit theory
Substrate induces a change of the active site of the enzyme
43
What does it mean that enzymes are stereospecific
Only one optical isomer will fit
44
Why are enzymes specific
Due to tertiary structure - specific shape needed to fit active site
45
Why are enzymes in washing powder
- Break down biological molecules in stains - break down by hydrolysis ➡️ makes them more water soluble so easier washed - allows powder to work at lower temp - more cost effective
46
What effect does pH have on enzyme activity
- optimal pH - if H+ added ➡️ active site protonated - if OH- added then active side deprotonated - changes structure of active site
47
What effect does temp have on enzyme activity
- optimal temp - changes active site - break interactions eg H bonds - v high = denatured