Amino Acids Flashcards

1
Q

What 2 functional groups are in Amino Acids?

A

Amino group and Carboxyl group

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2
Q

What makes each amino acid different?

A

R groups: side chains

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3
Q

What is a peptide bond?

A

1 amino acid’s carboxyl group bonds with another’s amino group

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4
Q

What do each of these mean: Dipeptide, Oligopeptide, and polypeptide.

A

Dipeptide: 2 monomers joined
Oligopeptide: many monomers joined
Polypeptide: more than 50 monomers joined (can make proteins)

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5
Q

Name the non-polar amino acids:

A

Aliphatic side chains: Glycine, Alanine, Valine, Leucine, Isoleucine

Methionine

Cysteine (can form disulphide bonds)

Aromatic: Phenylalanine, Tryptophan

Proline (link to alpha-amino group)

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6
Q

What bonds can non-polar amino acids form?

A

No hydrogen bonds (hydrophobic)

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7
Q

Name the polar amino acids:

A

Alcohols: Serine, Threonine, Tyrosine

Asparagine, Glutamine (amides of aspartate and glutamate)

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8
Q

What minds do polar amino acids make?

A

Hydrogen bonds not ionic

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9
Q

Name the charged amino acids:

A

Acidic: Aspartame, Glutamate

Basic: Lysine, Histidine, Arginine

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10
Q

What bonds can be made in charged amino acids?

A

Hydrogen bonds and ionic bonds

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11
Q

What are the ends of the proteins?

A

N-terminus (amino group) and C-terminus (carboxyl group)

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12
Q

What bonds in a polypeptide chain are flexible and which is rigid?

A

Single bonds are flexible and double bods are rigid but the polypeptide chain itself is flexible

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13
Q

Describe the secondary structure of an amino acid:

A

Interactions within polypeptide backbone

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14
Q

What types of secondary structures are there?

A

Alpha helix: hydrogen bonds every 3 residues; form of a helix

Beta Pleated sheets: 2 strands folded back and forth forming hydrogen bonds across

Random coil: joins 2 structures but has no structure itself

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15
Q

What are tertiary structures?

A

Interactions of side chains (R-groups)

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16
Q

What types of bonds are there in the tertiary structure of the amino acids?

A

Hydrogen bonds, ionic bonds, disulphide bonds and hydrophobic interactions between R-groups

17
Q

Describe the Quaternary structure of an amino acid:

A

More than 1 polypeptide chain; interactions between 2 or more subunits of a protein

18
Q

What is a native protein?

A

Correctly folded protein and has bonds

19
Q

What do you called an unfolded protein? How are the bonds within broken?

A

Denatured proteins. Bonds are broken by putting in energy

20
Q

What is a way to analyze proteins?

A

Polyacrylamide gel

21
Q

Describe a fatty acid binding protein

A

Hydrophobic tail and a polar head with a negative charge

22
Q

How do we know the structure? Describe the steps.

A

X-ray crystallography

Single crystal gives diffraction pattern which gives the electron density map and then finally you can determine the protein model