Biochemistry Chapter 1: Amino Acids, Peptides and Proteins Flashcards

1
Q

What are the 4 groups attached to the alpha-carbon?

A

R group, carboxylic acid group, amino group & a hydrogen

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2
Q

What is the stereochemistry for all amino acids in eukaryotes?

A

L

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3
Q

Where are D amino acids found?

A

They can exist in prokaryotes

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4
Q

Which amino acid does not have an S configuration?

A

cysteine

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5
Q

All amino acids are chiral except…

A

glycine (H)

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6
Q

What are the nonpolar, nonaromatic amino acids?

A

glycine, alanine, valine, leucine, isoleucine, methionine, proline

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7
Q

What are the aromatic amino acids?

A

tryptophan, phenylalanine, tyrosine

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8
Q

What are the polar amino acids?

A

serine, threonine, asparagine, glutamine, cysteine

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9
Q

What are the acidic amino acids?

A

aspartate, glutamate

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10
Q

What are the basic amino acids?

A

lysine, arginine, histidine

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11
Q

What does amphoteric mean?

A

They can accept or donate protons

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12
Q

what is the pka?

A

the pH at which half of the species is deprotonated; (HA) = (A-)

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13
Q

At low pH, the amino acid is…

A

Fully protonated

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14
Q

At pH near pI, the amino acid is…

A

a neutral zwitterion

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15
Q

at high pH, the amino acid is…

A

fully deprotonated

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16
Q

How can the isoelectric point, pI, be calculated?

A

calculating the average of the two pKa values

17
Q

How can you tell the pKa from a titration curve? pI?

A

flat at pka values & nearly vertical at the pI

18
Q

Amino acids without charged side chains have a pI around…

A

6

19
Q

Acidic amino acids have a pI…

A

Well below 6

20
Q

Basic amino acids have a pI…

A

Well above 6

21
Q

How is a peptide bond formed?

A

condensation or dehydration; the nucleophilic amino group of one amino acid attacks the electrophilic carbonyl group of another amino acid

22
Q

Why are amide bonds rigid?

A

resonance

23
Q

How do you break a peptide bond?

A

hydrolysis

24
Q

What amino acid can interrupt secondary structure of a protein?

A

Proline because of its rigid cyclic structure

25
Q

What can lead to protein denaturation?

A

heat and increasing solute concentration