Unit 4.7 Amino Acids Flashcards by Shirou Aizen

WELCOME

get out

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Define amphoteric

Can react both as base and acid

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Define zwitterion
(3 things)

Dipolar ion
Both positive & negative charge
Resulting in neutral molecule

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

H₂N on the left
COOH on the right
Quite obscure…

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

It’s on the α-carbon
to the carboxylic acid

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

CHR(NH₂)COOH

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

Lol

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

Glycine
R group is just H

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Draw structural formula of glycine “3D”
(Whiteboard

Stage is urs per se?

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

Lone pair on nitrogen can act as a base
Accepting a proton/donating an electron pair

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What allows the amino acid to be amphoteric?

Base (Nitrogen lone pair)
Acid (Carboxylic acid prob)

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

Alas, the zwitterion

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

The stage is always urs

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

Much higher up
Can form ionic bonds with neighboring ions
Due to charge

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

Can do hydrogen bonds
They’re polar molecules
Dissolves within water

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

Based on chain length
Length ∝ 1/solubility

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Define isoelectric points
(2-way)

The pH value at which
the molecule carries no electric charge

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The biggest regret, not listening

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

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What is a zwitterion?

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

Turn their OH
… an O^-
More H into the N (⁺NH₃)

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

O^- to OH
NH₂ to N^{+^H₃}

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

O^- stays the same
N⁺₃ to NH₂

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Show me the amide group?

-NH-C(=O)-

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

Dipeptides

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

- 2 amino acids joining up - Via condensation reaction

Define condensation reaction? (3-way)

- Formation of an ester - and a small molecule - e.g. H₂O

Ala = ? (Amino acid variation)

-CH₃

Gly = ? (Amino acid variation)

-H

Ser = ? (Amino acid variation)

-CH₂OH

Phe = ? (Amino acid variation)

-CH₂-BENZENE

Asp = ? (Amino acid variation)

-CH₂-COOH

Cys = ? (Amino acid variation)

-CH₂-SH

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

Stage is yours

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

Stage is yours again

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

Condensation polymerisation

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

How lazy of u

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

- 20 different amino acids - can form a large number - of formations/combinations

What are the 3 protein structures?

- Primary - Secondary - Tertiary

Simple definition of primary structure? (Protein structure)

Amino acid sequence

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

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

Wha

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

What are the 2 common types of secondary protein structures?

- α-helix - β-pleated sheet

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

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

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

- Overall folding of the chain - with interactions such as...

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

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

- By interactions between the side chains... - the "R" groups

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

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⁺

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

- Hydrogen bonds forming between - H and O in different R groups

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

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

- Between 2 cysteine - as they contain an R group of - CH₂SH

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

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

- Enzymes - aka biological catalysts

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

- Lowers activation energy - by offering an alternate pathway

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

1. Brewing 2. Dairy 3. Laundry

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

... Yeast.

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

... Fermentation process .... create cheese and yoghurt

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

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