Lecture 2 DA Flashcards

1
Q

According to the DL system, what are most proteins/amino acids in the human body?

A

L form
Bacterial walls can have D proteins hence their toxicity.
Antibiotics are based off D proteins/amino acids.

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2
Q

What is an enantiomer?

A

Mirror images, non-imposable

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3
Q

What is hydropathy?

A

Activation energy needed to pull a molecule from a hydrophobic phase to water.

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4
Q

What happens if the hydropathy of a molecule is positive? What about negative?

A

Positive - hydrophobic

Negative - hydrophilic

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5
Q

What is the molecular weight of a free amino acid? What about in proteins? Why the difference?

A

Free - 128
Protein - 110
Due to the loss of water in condensation.

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6
Q

What are the non-polar, aliphatic amino acids (7)?

A
Gycine
Alanine
Proline
Valine
Leucine
Isoleucine
Methionine
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7
Q

What are the aromatic amino acids (3)?

A

Phenylalanine
Tyrosine
Tryptophan

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8
Q

What are the positively charged amino acids (3)?

A

Lysine
Arginine
Histidine

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9
Q

What are the negatively charged amino acids (2)?

A

Aspartate

Glutamate

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10
Q

What is cystine?

A

Polymer of cysteine, forms a disulphide bridge.

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11
Q

What is the most common way to regulate proteins?

A

Phosphorylation

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12
Q

Name 2 amino acid like structures not found in proteins.

A

Orthonin

Citrulline

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13
Q

What wavelength do aromatic structures absorb?

A

280nm

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14
Q

What is amphoteric?

A

Dual acid-base behaviour, amino acids are amphoteric.

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15
Q

What form do amino acids exist at their pI?

A

Zwitterionic form, in most cases

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16
Q

Can amino acids buffer?

A

Yes

17
Q

What loses its H+ first, the COOH or NH3, and explain why (2).

A

COOH first-The positive charge on the NH3 repels it.-As amino acids tend towards neutrality, losing the COOH H+ ion will mean a negative charge to offset the NH3+ positivity.

18
Q

Which amino acid has the highest buffering capacity, and why?

A

Histidine, its pI is closest to 7.2.