Amino acids Flashcards

1
Q

How do proteins become functional?

A

they must fold, forming complex 3D shapes in order

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2
Q

What is also necessary with proteins?

A

post-translational modifications (PMTs)

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3
Q

What must happen to a protein to allow it to carry out it’s function?

A

it must remain stable for a period of time

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4
Q

What group determines the properties of the 20 amino acids?

A

the R group

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5
Q

What shape are amino acids?

A

Tetrahedral

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6
Q

How could the symmetry of amino acids be described?

A

chiral (asymmetrical)

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7
Q

Is L-Alanine or D-Alanine in all amino acids?

A

L-Alanine

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8
Q

How can you tell the difference between L-Alanine and D-Alanine?

A

use the CORN rule:

  • place the hydrogen at the back of the molecule.
    -In an anti-clockwise direction the groups read CO-R-N (For L-Alanine).
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9
Q

Name the 5 amino acid groups

A
  • Hydrophobic
    -Aromatic
    -Polar
    -Negatively charged
    -Positively charged
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10
Q

Define amphipathic

A

contains both hydrophilic and hydrophobic properties

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11
Q

Name all of the hydrophobic amino acids

A

-Glycine
-Alanine
-Valine
-Leucine
-Isoleucine
-Methionine
-Proline

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12
Q

Describe Aromatic amino acids

A

-all contain a ring of delocalised electrons
-hydrophobic ring
-two are hydrophobic and the third is amphipathic

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13
Q

What is the most common amino acid?

A

Leucine

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14
Q

Describe Valine and it’s letter

A

V
-small hydrophobic amino acid often found in the hydrophobic core of globular proteins.

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15
Q

What amino acid is most common replacement in mutation?

A

Alanine

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16
Q

Describe methionine and it’s letter

A

M
- contains a sulfur
-unreactive
- often the first amino acid in an unmodified protein (as it is the initiation codon).

17
Q

Describe Proline and it’s letter

A

P
- ring limits conformation of backbone
-can sometimes be found in cis conformation
-IMINO ACID (lacks 1 hydrogen on the amine group).

18
Q

Describe phenylalanine, what is it’s letter?

A

F
-has phenyl group (aromatic ring).
-ring is unreactive and hydrophobic
-weakly absorbs UV light.

19
Q

Describe Tyrosine and it’s letter

A

Y
-polar OH group, can make hydrogen bonds
-Hydrophobic ring
-overall amphipathic
-absorbs light at 280 nm

20
Q

Describe Tryptophan and it’s letter

A

W
-largest amino acid
-weak hydrogen bonding to the NH makes it amphipathic
-strongly absorbs light at 280nm
-fluorescent

21
Q

Describe polar groups

A
  • have polar side chains or partially charged side chains
  • hydrophilic and often found on the surface of proteins
22
Q

Name all of the polar amino acids

A
  • Serine
    -Threonine
  • Cysteine
    -Asparagine
    -Glutamine
23
Q

Describe Serine

A

S
- both have alcohol groups
-usually on protein surface
- Serine is smaller primary alcohol and most common replacement in mutations.
-often phosphorylated in proteins

24
Q

Describe Threonine

A

T
- secondary alcohol
- often phosphorylated in proteins

25
Describe Cysteine and it's letter
C - reactive sulfhydryl group -can cross link with other cysteines to form disulphide bonds (strong covalent bonds).
26
What is the difference between Asparagine and Glutamine?
one has an extra CH2 group
27
What are the similarities between Asparagine and Glutamine?
- both found on the surface -can form many hydrogen bonds - both very similar to their acidic counterparts
28
Describe negatively charged amino acids
-Acids -Almost always deprotonated -Charged state
29
Name all of the charged amino acids. What are they're letters?
-Aspartate (N) -Glutamate (Q)
30
What will Aspartate and Glutamate be at physiological PH?
-deprotonated charged -Glutamate creates Umami taste
31
Describe positively charged amino acids
-can act as bases -two of the three almost always protonated and charged at physiological PH.
32
Name all of the positively charged Amino acids
-Lysine (K) -Arginine (R) -Histidine (H).
33
Describe Lysine and it's letter
K - below PH 10.5 -amide group will be NH3+ -may be acylated to regulate protein
34
Describe Arginine and it's letter
R - below PH 12.5, the guanadino group will be changed
35
What is a key structural feature of histidine?
imidazole ring
36
How does histidine act in biological systems?
as a buffer
37
Why is histidine often added to recombinant proteins?
To act as a purification tag.
38
How would you describe a Glutamate to Valine replacement at position 6?
It would be called an E6V mutant.
39