Amino Acid & Protein Structure Flashcards

1
Q

What are proteins are present in enamel and what is their function?

A

Amelogenins

Enamelins

Framework for mineralisation

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2
Q

What are proteins are present in dentin? (3)

A

Collagen

Glycoproteins

Proteoglycans

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3
Q

What are proteins are present in cementum? (2)

A

Collagen

Glycoproteins

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4
Q

What determines the structure of a protein?

A

DNA sequence

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5
Q

Describe and explain the structure of a protein formed by spontaneous folding up of a linear amino acid chain (side chains).

A

Non polar side chains = hydrophobic = core region

Polar side chains = hydrophilic = on outside of molecule (forms H-bonds with water)

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6
Q

What amino acid enantiomer is found in nature?

A

L

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7
Q

Which amino acid does not display optical isomerism?

A

Glycine

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8
Q

What bond links two amino acids?

A

Peptide bond

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9
Q

Which amino acid can be both hydrophilic and hydrophobic?

A

Tyrosine

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10
Q

What is special about cysteine?

A

Able to form disulfide bonds (cystine)

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11
Q

What is special about proline?

A

Side chain is continuous with alpha amino group (constrains protein structure)

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12
Q

Why do we draw the amino group on the left hand side (start from N-terminal)?

A

Reflects process of translation

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13
Q

Give three features of the peptide bond

A

Shorter than expected

Rigid (no rotation around bond)

Trans arrangement

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14
Q

What are the partial charges in the amide link?

A

Partial negative charge on oxygen

Partial positive charge on nitrogen

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15
Q

What type of reaction is the formation of a disulphide bridge?

A

Oxidation

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16
Q

What could you use to break a disulphide bridge?

A

Reducing agent

17
Q

Give an example of a dipeptide used in food.

A

Aspartame - artificial sweetener Asp-Phe

18
Q

Give an example of a tripeptide

A

Glutathione - natural antioxidant Glu-Cys-Gly

19
Q

Give two examples of short polypeptides

A

Glucagon (peptide hormone) - 29AA

Substance P (neurotransmitter) - 10AA

(10-40 AA)

20
Q

Give an example of a large protein

A

Dystrophin - 3684 AA, 427kDa

21
Q

What is the primary protein structure?

A

Sequence of amino acids in polypeptide chain

22
Q

What is the secondary protein structure?

A

Folding/coiling of polypeptide chain (alpha helix/beta pleated sheet)

23
Q

What is the tertiary protein structure?

A

Polypeptide chain folds upon itself further

24
Q

What is the quaternary protein structure?

A

Folded polypeptide chains join together