3.1.4 Proteins Flashcards

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1
Q

Monomers of proteins

A

Amino acid -> polypeptide -> protein

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2
Q

How many amino acids are there?

A

100

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3
Q

How many amino acids occur in living organisms?

A

20

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4
Q

What does each amino acid differ by?

A

The R group

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5
Q

Components of an amino acid

A
  • R group
  • Carboxyl group
  • Amino group
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6
Q

Amino acid: R group

A
  • Side chain
  • Variety of different chemical groups different for each amino acid
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7
Q

Amino acid: Carboxyl (COOH) group

A

an acidic group which gives the amino acid the acid part of its name

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8
Q

Amino acid: amino (NH2) group

A

basic group where the amino part of the name amino acid comes from

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9
Q

Formation of proteins

A
  • Condensation reaction between 2 amino acids forms a peptide bond (between the -OH of the carboxyl group and the -H of the amino group of another amino acid)
  • NH2 joins to COOH
  • There is a free NH2 at one end and a free COOH group at another end
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10
Q

Dipeptide

A

Formed by the condensation of 2 amino acids

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11
Q

Polypeptides

A

Formed by the condensation of many amino acids

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12
Q

4 structure stages of proteins

A
  • Primary
  • Secondary
  • Tertiary
  • Quaternary
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13
Q

Primary structure of proteins

A
  • The order and number of amino acids in a protein
  • Contains initial sequence of amino acids + so determines the protein’s function and 3d shape
  • Specific for each protein (small alteration can affect protein function
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14
Q

Secondary structure of proteins

A
  • The shape of the amino acid chain
  • Hydrogen bonds form between the H of the -NH (overall positive charge) and the O of the C=O (overall negative charge)
  • This causes the polypeptide chain to be twisted into a 3D shape (either alpha helix or beta pleated)
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15
Q

Tertiary structure of proteins

A
  • Interactions between R groups
  • 3D shape of the protein (makes each protein distinct and recognisable)
  • Further twisting + folding
  • Disulfide bridges, ionic bonds and hydrogen bonds form
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16
Q

Tertiary structure: Disulfide bridges

A

Fairly strong, not easily broken

17
Q

Tertiary structure: Ionic bonds

A

Formed between any carboxyl and amino groups that are not involved in forming peptide bonds

18
Q

Tertiary structure: Hydrogen bonds

A

Numerous, but easily broken

19
Q

Tertiary bonds in terms of strength

A
  1. Disulfide bridges
  2. Ionic bonds
  3. Hydrogen bonds
20
Q

Quaternary structure of proteins

A

Present in proteins with more than 1 polypeptide chain

21
Q

Test for proteins

A
  1. To a test tube add equal amounts of liquid sample and sodium hydroxide (to make it alkaline)
  2. Add biuret reagant
  3. If protein is present, colour change: blue -> purple
22
Q

Biuret reagent

A

Add few drops of dilute copper (II) sulfate solution

23
Q

Types of proteins

A
  • Globular proteins (have metabolic functions)
  • Fibrous proteins (have structural functions)
24
Q

How many polypeptides does a simple protein contain?

A

1

25
Q

How many polypeptides does a functional protein contain

A

1 or more polypeptides

26
Q

Fibrous proteins

A
  • Long polypeptide chains which run parallel to each other, and have cross-linkages between them -> stable
27
Q

Examples of fibrous proteins

A
  • Collagen
  • Keratin
28
Q

Globular proteins

A

Compact, roughly spherical shape

29
Q

Examples of globular proteins

A
  • Haemoglobin and enzymes (these are conjugated proteins because they also contain a non-protein chemical group)
30
Q

What is the structure of a protein determined by?

A

position of amino acid, therefore the primary structure

31
Q

Similarities between amino acids

A
  • NH2
  • COOH
32
Q

Difference between amino acids

A

different R groups