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A Chem Finale pt 1. > Unit 4.7 Amino Acids > Flashcards

Unit 4.7 Amino Acids Flashcards

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1
Q

WELCOME

A

get out

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2
Q

Define amphoteric

A

Can react both as base and acid

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3
Q

Define zwitterion
(3 things)

A
  • Dipolar ion
  • Both positive & negative charge
  • Resulting in neutral molecule
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4
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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5
Q

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

A
  • It’s on the α-carbon
  • to the carboxylic acid
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6
Q

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

A

CHR(NH2)COOH

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7
Q

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

A

Lol

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8
Q

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

A
  • Glycine
  • R group is just H
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9
Q

Draw structural formula of glycine “3D”
(Whiteboard

A

Stage is urs per se?

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10
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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11
Q

What allows the amino acid to be amphoteric?

A
  • Base (Nitrogen lone pair)
  • Acid (Carboxylic acid prob)
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12
Q

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

A

Alas, the zwitterion

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13
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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14
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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15
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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16
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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17
Q

Define isoelectric points
(2-way)

A
  • The pH value at which
  • the molecule carries no electric charge
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18
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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19
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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20
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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21
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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22
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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23
Q

Show me the amide group?

A

-NH-C(=O)-

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24
Q

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

A

Dipeptides

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25
Q

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

A
  • 2 amino acids joining up
  • Via condensation reaction
26
Q

Define condensation reaction?
(3-way)

A
  • Formation of an ester
  • and a small molecule
  • e.g. H2O
27
Q

Ala = ?
(Amino acid variation)

A

-CH3

28
Q

Gly = ?
(Amino acid variation)

A

-H

29
Q

Ser = ?
(Amino acid variation)

A

-CH2OH

30
Q

Phe = ?
(Amino acid variation)

A

-CH2-BENZENE

31
Q

Asp = ?
(Amino acid variation)

A

-CH2-COOH

32
Q

Cys = ?
(Amino acid variation)

A

-CH2-SH

33
Q

Draw the formation eqn of a dipeptide from alanine and alanine
(Whiteboard)

A

Stage is yours

34
Q

Draw the formation eqn of a dipeptide from a glycine and glycine
(Whiteboard)

A

Stage is yours again

35
Q

What type of reaction takes place for the formation of polypeptides?

A

Condensation polymerisation

36
Q

Just, well, generally know how polypeptides are formed, linked, chained, whatever

A

How lazy of u

37
Q

Explain the huge variety of different proteins
(3-way)

A
  • 20 different amino acids
  • can form a large number
  • of formations/combinations
38
Q

What are the 3 protein structures?

A
  • Primary
  • Secondary
  • Tertiary
39
Q

Simple definition of primary structure?
(Protein structure)

A

Amino acid sequence

40
Q

What are primary structures?
(Protein structures)
(2-way + 2-way)

A
  • Takes consideration the order of
  • amino acids in chain
  • Structure held together by covalent bonds
  • such as peptide bonds
41
Q

Simple definition of secondary structure?
(Protein structure)
(LIL CHECK UP NOOOOO)

A

Wha

42
Q

What are secondary structures?
(Protein structures)
(3-way)

A
  • Defined by pattern of hydrogen bonds
  • between amine hydrogen and carbonyl oxygen atoms
  • in peptide back bone
43
Q

What are the 2 common types of secondary protein structures?

A
  • α-helix
  • β-pleated sheet
44
Q

Describe secondary, α-helix?
(Protein structures…. secondary edition)
(1 thing +
2-way +
3-way)

A
  • 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
45
Q

Describe secondary, β-pleated sheet?
(Protein structures… secondary edition)
(2-way +
4-way)

A
  • 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
46
Q

Simple definition of tertiary structure?
(Protein structures)
(2-way…)

A
  • Overall folding of the chain
  • with interactions such as…
47
Q

What are tertiary structures?
(Protein structures)
(1 + () + 2-way)

A
  • A description of the way the whole chain
  • (including secondary structure)
  • folds itself into its
  • final 3-dimensional shape
48
Q

How is the tertiary structure of a protein held together?
(Protein structures)
(2-way)

A
  • By interactions between the side chains…
  • the “R” groups
49
Q

What are the 4 interactions that there may be in tertiary structures?
(Protein structures)

A
  • Ionic interactions
  • Hydrogen bonds
  • Van der Waals dispersion forces
  • Sulfur bridges
50
Q

Explain ionic interactions?
(Protein structures… tertiary interactions)
(2-way + 2-way)

A
  • Due to additional acid or amine groups
  • within the R groups
  • Proton exchange can occur leaving
  • COO- and NH3+
51
Q

Explain hydrogen bonds?
(Protein structures… tertiary interactions)
(2-way… hm)

A
  • Hydrogen bonds forming between
  • H and O in different R groups
52
Q

Explain Van der Waals dispersion forces?
(Protein structures… tertiary interactions)
(3-way)

A
  • Large R groups containing
  • lots of electrons that can
  • cause these temporary dipoles
53
Q

Explain sulfur bridges?
(Protein structures… tertiary interactions)
(3-way)

A
  • Between 2 cysteine
  • as they contain an R group of
  • CH2SH
54
Q

Explain why hydrogen bonding occurs in secondary protein structures, such as in an α-helix?
(Protein structures per se)
(3 things)

A
  • 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
55
Q

What is the role of proteins in living systems?
(2 things)

A
  • Enzymes
  • aka biological catalysts
56
Q

How does an enzyme speed up the rate of a chemical reaction?
(2-way)

A
  • Lowers activation energy
  • by offering an alternate pathway
57
Q

What are the 3 ways enzymes are needed in typical industry?

A
  1. Brewing
  2. Dairy
  3. Laundry
58
Q

Explain brewing and it’s enzyme importance?
(Prob check up, but don’t sell)

A

… Yeast.

59
Q

Explain dairy and it’s enzyme importance?
(Still check up, don’t sell as well)

A

… Fermentation process
…. create cheese and yoghurt

60
Q

Explain laundry and it’s enzyme importance?
(Check per se, what does per se even mean)

A
  • Biological washing powder
  • Something to do with how they eat up oils and fats
  • In addition, save money by not needing heat
61
Q

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

A

Correct

A Chem Finale pt 1. (10 decks)

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