Lecture 12 Flashcards

1
Q

What is the charge of Lysine at pH 7?

A

It is positively charged because of the amino group in the side chain

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2
Q

What does the side chain of Lysine contain?

A

A positively charged side chain

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3
Q

What kind of H bonds is the side chain of Lysine capable of forming?

A

It is an H-bond donor through its amino group at neutral pH’s

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4
Q

What is the Polarity of Lysine?

A

It is very polar

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5
Q

What is the pKa of the amino group in the R group of Lysine?

A

It has a pKa of 10

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6
Q

What charge does Lysine have at pH 7?

A

A positive charge

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7
Q

Why does Lysine have a positive charge at pH 7?

A

Because it has an NH3 group

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8
Q

Why is Lysine know as a basic amino acid?

A

Because it exists as a base at neutral pH through it amino group

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9
Q

What is the charge of Arginine at pH 7?

A

It is positively charged

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10
Q

What is a Guanido group?

A

The end part of the R group of arginine

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11
Q

What is the pKa of the NH2 of Arginine?

A

12.5

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12
Q

Why is it difficult to deprotonate the functional group of Arginine?

A

Because it is very stable due to resonance

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13
Q

Why can Arginine be described as a basic amino acid?

A

Because the side chain is neutral when it is in the base form

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14
Q

What is the polarity of arginine?

A

It is very polar

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15
Q

What is the H-bond capability of Arginine?

A

It is an H-bond donor

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16
Q

What are the exceptions for the amino acid abbreviation rules?

A
  • Asparagine (Asn)
  • Glutamine (Gln)
  • Isoleucine (Ile)
  • Tryptophan (Trp)
17
Q

Where are Polar side chains usually found?

A

In proteins on the surface where they can interact with water

18
Q

Where are non-polar side chains usually found?

A

Buried in the protein core to minimize interaction with water

19
Q

Which parts of the amino acid is a peptide bond between?

A

The carboxyl of one amino acid and the amino group of another amino acid

20
Q

What is removed in the formation of a peptide bond?

A

Two H’s from the amino group and one O from the carboxyl group to form a water

21
Q

What is the symmetry of the bond that connects amino acids together?

A

It is asymmetrical

22
Q

What does the N-terminal describe?

A

The presence of a free amino group

23
Q

What does the C-terminal describe?

A

The presence of a C terminal on one end

24
Q

What is a Dipeptide, Tripeptide, Tetrapeptide, Pentapeptide?

A

Two amino acids, three amino acids, four amino acids, five amino acids

25
What is an Oligopeptide?
The general term for a larger number of amino acids, often refers to synthetic. peptides
26
What is a Polypeptide?
A long chain of amino acids, usually produced naturally
27
What is a Protein?
A large polypeptide a with a biological function
28
What retains their charge in a peptide?
* Terminal amino group (+1) * Carboxylate group (-1) * Side chains (if they have one)
29
How are the number of connected amino acids related to the peptide bond?
There will always be one less peptide bond than amino acids
30
What is the Primary Structure?
The sequence of amino acids in a polypeptide
31
What joins each amino acid to the next?
A covalent peptide bond
32
From which terminus do we read polypeptide chains?
From N-terminus to C-terminus
33
Where is no rotation permitted in peptide bonds?
Rotation is not permitted around the C-N bond because of the double bond character
34
In a peptide bond, which atoms are found in the same plane?
* Two Alpha carbons * Carbonyl carbon * Oxygen * Nitrogen * Hydrogen on the nitrogen
35
What are the three kinds of bonds in a peptide bond?
* N - Calpha * Calpha - carbonyl carbon * Carbonyl carbon - nitrogen
36
Which bonds in a peptide bond allow for rotation?
N - Calpha and C-alpha to Carbon of the carbonyl
37
What does the Primary structure determine?
The 3D structure
38
Why is the folding conformations of polypeptides limited?
Due to steric hindrance
39
What is the hydrogen bonding potential of a peptide bond?
The carbonyl and N-H can hydrogen bond with each other