Amino acids Flashcards

1
Q

What different types of proteins are there?

A

Structural, signalling, enzymes, antibodies, receptors

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2
Q

How can enzymes be used in biochem?

A

Can detect specific proteins through techniques of: Western blotting; Enzyme linked immunosorbent assay

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3
Q

What are the roles of receptors?

A

Bind to molecules which send signals to cell (insulin receptor); allow molecules to enter cell (CD36); detect changes in surrounding environment (mechanoreceptors detect changes in blood pressure and flow)

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4
Q

How can proteins be identified?

A

Centrifugation then gel electrophoresis; comparison of different samples allows determination of changes in protein level and interaction

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5
Q

What characteristics of a sample can assessed in comparison?

A

Concentration in a sample; types of proteins present; functions of proteins

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6
Q

How many amino acids are there?

A

20

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7
Q

How can amino acids be classified by structure?

A

Non-polar aliphatic; aromatic; non-polar; polar uncharged, negatively charge; positively charged; non-charged N-containing; hyroxyl-containing; S-containing

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8
Q

What are amino acids that are key to polypeptide structure and function?

A

Cystein forms disulfide bonds; serine is most commonly phosphorylated amino acid; methionine is always the first amino acid

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9
Q

What is the primary structure?

A

Chain of amino acids; read from N- to C- terminus (NH2 end to COOH end)

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10
Q

What is the secondary structure?

A

Folding of polypeptide chain; formed of H bonds

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11
Q

What are two types of secondary structure?

A

alpha-helix and beta-pleated sheet

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12
Q

What are the characteristics of alpha helix?

A

H bond each 4th amino acid between C=O and N-H; 3.6 amino acid resides/turn

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13
Q

What is an example of an alpha helix?

A

Myogoblin

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14
Q

What are the characteristic of beta pleated sheet?

A

H bond form between peptide bonds; either parallel (between different chains) or anti-parallel (between same chain); multiple sheets provide stability

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15
Q

What is an example of beta pleated sheet?

A

Silk fibroin

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16
Q

What is the tertiary structure?

A

The spatial arrangement of amino acids formed by folding of secondary structure; enables protection, interaction, and function; gives proteins their final conformations

17
Q

What bonds stabilise the tertiary structure?

A

Electrostatic, hyrophobic/philic, H bonds, disulfide bridges

18
Q

What is the Quaternary structure?

A

Arrangement and interaction within multiple polypeptide chains; can involve interactions between R groups

19
Q

What are proteins that have Quaternary structure?

A

Hb and insulin