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A Chem Finale pt 1. > Unit 4.7 Amino Acids (re-run) > Flashcards

Unit 4.7 Amino Acids (re-run) Flashcards

(60 cards)

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1
Q

Define amphoteric

A

Can react both as base and acid

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2
Q

Define zwitterion
(3 things)

A
  • Dipolar ion
  • Both positive & negative charge
  • Resulting in neutral molecule
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3
Q

How can u tell it’s an α-amino acid?
(3 things)

A
  • H2N on the left
  • COOH on the right
  • Quite obscure…
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4
Q

What classifies an α-amino acid?
(2-way)

A
  • It’s on the α-carbon
  • to the carboxylic acid
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5
Q

What is the general formula for an α-amino acid?

A

CHR(NH2)COOH

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6
Q

Draw displayed formula of general formula for an α-amino acid
(Whiteboard)

A

Lol

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7
Q

What is the simplest amino acid?
(2-tings)

A
  • Glycine
  • R group is just H
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8
Q

Draw structural formula of glycine “3D”
(Whiteboard

A

Stage is urs per se?

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9
Q

How does the presence of an amine group allow amino acids to also act as a base?
(2-way)

A
  • Lone pair on nitrogen can act as a base
  • Accepting a proton/donating an electron pair
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10
Q

What allows the amino acid to be amphoteric?

A
  • Base (Nitrogen lone pair)
  • Acid (Carboxylic acid prob)
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11
Q

Show with a diagram, the amphoteric behaviour glycine
State what the result is?

A

Alas, the zwitterion

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12
Q

Draw the zwitterion version of alanine (R=CH3)
(Whiteboard)
(Just use that as foundation incase of other “zwitterions”)

A

The stage is always urs

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13
Q

Explain whether m.p of amino acid is high or low?
(3 things)

A
  • Much higher up
  • Can form ionic bonds with neighboring ions
  • Due to charge
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14
Q

How are amino acids also soluble in water?
(3 things)

A
  • Can do hydrogen bonds
  • They’re polar molecules
  • Dissolves within water
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15
Q

How can different amino acids have different solubility?
(1 thing, 1 imp)

A
  • Based on chain length
  • Length ∝ 1/solubility
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16
Q

Define isoelectric points
(2-way)

A
  • The pH value at which
  • the molecule carries no electric charge
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17
Q

The biggest regret, not listening

A

I’ll somehow draw this BUT, hopefully that next specific lesson comes in clutch man

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18
Q

What is a zwitterion?

A

Idk the full real answer… BUT:
- seems to be the “isoelectric point”???
- In the amino acids, the ones with an electron negative O- (Dipole type shi)
- Involves with the different pH (acidic and alkaline type shi)

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19
Q

How to draw the zwitterion versions of an amino acid?
(2-way)

A
  • Turn their OH
  • … an O-
  • More H into the N (+NH3)
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20
Q

What may happen to a zwitterion of an amino acid if turned more acidic?
(2 things)

A
  • O- to OH
  • NH2 to N+H3
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21
Q

What may happen to a zwitterion of an amino acid if turned more alkaline?
(2 things)

A
  • O- stays the same
  • N+3 to NH2
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22
Q

Show me the amide group?

A

-NH-C(=O)-

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23
Q

What’s the amide group called in the “biology section”?

A

Dipeptides

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24
Q

How is an amide group formed?
(or dipeptide if u want)

A
  • 2 amino acids joining up
  • Via condensation reaction
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25
Define condensation reaction? (3-way)
- Formation of an ester - and a small molecule - e.g. H2O
26
Ala = ? (Amino acid variation)
-CH3
27
Gly = ? (Amino acid variation)
-H
28
Ser = ? (Amino acid variation)
-CH2OH
29
Phe = ? (Amino acid variation)
-CH2-BENZENE
30
Asp = ? (Amino acid variation)
-CH2-COOH
31
Cys = ? (Amino acid variation)
-CH2-SH
32
Draw the formation eqn of a dipeptide from alanine and alanine (Whiteboard)
Stage is yours
33
Draw the formation eqn of a dipeptide from a glycine and glycine (Whiteboard)
Stage is yours again
34
What type of reaction takes place for the formation of polypeptides?
Condensation polymerisation
35
Just, well, generally know how polypeptides are formed, linked, chained, whatever
How lazy of u
36
Explain the huge variety of different proteins (3-way)
- 20 different amino acids - can form a large number - of formations/combinations
37
What are the 3 protein structures?
- Primary - Secondary - Tertiary
38
Simple definition of primary structure? (Protein structure)
Amino acid sequence
39
What are primary structures? (Protein structures) (2-way + 2-way)
- Takes consideration the order of - amino acids in chain - Structure held together by covalent bonds - such as peptide bonds
40
Simple definition of secondary structure? (Protein structure) (LIL CHECK UP NOOOOO)
Wha
41
What are secondary structures? (Protein structures) (3-way)
- Defined by pattern of hydrogen bonds - between amine hydrogen and carbonyl oxygen atoms - in peptide back bone
42
What are the 2 common types of secondary protein structures?
- α-helix - β-pleated sheet
43
Describe secondary, α-helix? (Protein structures.... secondary edition) (1 thing + 2-way + 3-way)
- Protein chain wound into a coil (like loose spring) - Coil runs in clockwise direction - as it goes away from you - Hydrogen from amide on one section of chain... - forms hydrogen bond with oxygen - from carbonyl group further along the chain
44
Describe secondary, β-pleated sheet? (Protein structures... secondary edition) (2-way + 4-way)
- Chains are folded - So they lie alongside each other - Likewise, hydrogen from amide on one section of chain... - forms hydrogen bond with oxygen - from carbonyl group - as chain folds back on itself
45
Simple definition of tertiary structure? (Protein structures) (2-way...)
- Overall folding of the chain - with interactions such as...
46
What are tertiary structures? (Protein structures) (1 + () + 2-way)
- A description of the way the whole chain - (including secondary structure) - folds itself into its - final 3-dimensional shape
47
How is the tertiary structure of a protein held together? (Protein structures) (2-way)
- By interactions between the side chains... - the "R" groups
48
What are the 4 interactions that there may be in tertiary structures? (Protein structures)
- Ionic interactions - Hydrogen bonds - Van der Waals dispersion forces - Sulfur bridges
49
Explain ionic interactions? (Protein structures... tertiary interactions) (2-way + 2-way)
- Due to additional acid or amine groups - within the R groups - Proton exchange can occur leaving - COO- and NH3+
50
Explain hydrogen bonds? (Protein structures... tertiary interactions) (2-way... hm)
- Hydrogen bonds forming between - H and O in different R groups
51
Explain Van der Waals dispersion forces? (Protein structures... tertiary interactions) (3-way)
- Large R groups containing - lots of electrons that can - cause these temporary dipoles
52
Explain sulfur bridges? (Protein structures... tertiary interactions) (3-way)
- Between 2 cysteine - as they contain an R group of - CH2SH
53
Explain why hydrogen bonding occurs in secondary protein structures, such as in an α-helix? (Protein structures per se) (3 things)
- O of C=O H-bonding to H on N-H - O of C=O and side chains - Amines and alcohols/carboxylic acids of side chains
54
What is the role of proteins in living systems? (2 things)
- Enzymes - aka biological catalysts
55
**How does an enzyme speed up the rate of a chemical reaction? (2-way)**
- Lowers activation energy - by offering an alternate pathway
56
What are the 3 ways enzymes are needed in typical industry?
1. Brewing 2. Dairy 3. Laundry
57
Explain brewing and it's enzyme importance? (Prob check up, but don't sell)
... Yeast.
58
Explain dairy and it's enzyme importance? (Still check up, don't sell as well)
... Fermentation process .... create cheese and yoghurt
59
Explain laundry and it's enzyme importance? (Check per se, what does per se even mean)
- Biological washing powder - Something to do with how they eat up oils and fats - In addition, save money by not needing heat
60
All u have is a major check up on zwitterion, not so much on that "simple def. of secondary structures". Otherwise tho, expect the unexpected
Correct

A Chem Finale pt 1. (12 decks)

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