2.2 Proteins Flashcards

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1
Q

What are globular proteins?

A

Proteins formed by compact amino acid chains, then folded into intricate chains that resemble spheres

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2
Q

Are globular proteins soluble or insoluble in water?

A

Soluble

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3
Q

Give an example of a globular protein and what it does:

A

Insulin, which is produced by the pancreas, it aids the bodies ability to regulate energy and metabolize sugars

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4
Q

What does insulin illustrate?

A

A proteins ability to act as a biological messenger

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5
Q

What else can proteins act as?

A

Biological transport mechanisms and they can play a role in the structure of animal cells

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6
Q

What are conjugated proteins?

A

(Non-polypeptide) Proteins that function in interaction with other chemical groups

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7
Q

What are conjugated proteins attached by?

A

They are attached by covalent bonds (weak interactions)

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8
Q

Are conjugated proteins soluble or insoluble in water?

A

Soluble in water

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9
Q

What are proteins?

A

Long chains of amino acids, they are a diverse group of large and complex molecules

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10
Q

Give an example of conjugated proteins:

A
  • haemoglobin

* catalase

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11
Q

What are fibrous proteins?

A

A proteins with a elongated shape forming a rod or wire like shape

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12
Q

What do fibrous proteins provide?

A

Structural support for cells and tissues

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13
Q

Give examples of fibrous proteins:

A
  • keratin
  • elastin
  • collagen
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14
Q

Are fibrous proteins soluble or insoluble in water?

A

Insoluble

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15
Q

What breaks down proteins?

A

Protease enzymes

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16
Q

What is a prosthetic group?

A

A non protein component in globular proteins

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17
Q

What are proteins without a prosthetic group called?

A

Simple proteins

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18
Q

What is formed when a lipid and protein combine?

A

A lypoprotein

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19
Q

What is a glycoprotein?

A

When a carbohydrate combines with a protein

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20
Q

What is a COFACTOR?

A

A prosthetic group formed by metal ions and vitamins

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21
Q

Give an example of a prosthetic group?

A

HAEM group - contain an iron ion

22
Q

What contains HAEM groups?

A

Catalase and haemoglobin

23
Q

What do protease enzymes break down?

A

Peptide bonds

24
Q

How does the protease enzyme denature the protein?

A

It breaks the bonds, altering the structure, it first breaks the hydrogen, then the ionic then the disulphide

25
Q

What changes in the structure of amino acids?

A

The R group changes, but all amino acids have the same general structure

26
Q

What are the four structures of proteins?

A
  • primary structure
  • secondary structure
  • tertiary structure
  • quaternary structure
27
Q

How many naturally occurring amino acids are there?

A

There are 20 naturally occurring amino acids each with their own R group

28
Q

How is a polypeptide chain formed?

A

When amino acids are added to a dipeptide

29
Q

How many polypeptides does one protein consist of?

A

One polypeptide

30
Q

What is polymerisation? And what type of reaction is this?

A

The process in which amino acid monomers are joined to form a polypeptide, this is a condensation reaction

31
Q

What are the types of proteins?

A
  • structural
  • catalytic
  • signalling
  • immunological
32
Q

What are structural proteins?

A

They are the main component of body tissues such as muscle, skin, hair and ligaments

33
Q

What are catalytic enzymes?

A

All enzymes are proteins catalysing many biochemical reactions

34
Q

What are signalling proteins?

A

Hormones and receptors (many of these are proteins)

35
Q

What are immunological proteins?

A

Antibodies are proteins

36
Q

Where is a disulphide bridge formed?

A

Between two cystine amino acids

37
Q

What does the primary protein structure look like? And what bond joined them?

A

A long chain of amino acids joined by polypeptide bonds

38
Q

What doe the primary structure of a protein determine?

A

It’s shape and function

39
Q

What are the two secondary structures?

A
  • alpha helix

* beta pleated sheet

40
Q

What bond does the secondary structure contain?

A

Weak hydrogen bonds

41
Q

How are the weak hydrogen bonds form?

A

The positive charge on the hydrogen and the negative charge of the oxygen

42
Q

What do the hydrogen bonds cause in the secondary structure?

A

Causes the long polypeptide chains to twist into a 3D helix

43
Q

What is the tertiary structure?

A

The 3rd protein structure it is a further folded and twisted to give it a more complex 3D structure

44
Q

How is the tertiary structure maintained?

A

By a number of bonds

45
Q

What bonds are contained in the tertiary structure?

A
  • disulphide bonds
  • ionic bonds
  • hydrogen bonds
46
Q

What are disulphide bonds?

A

Bridges formed between cystine they are strong and difficult to break

47
Q

What are ionic bonds?

A

Bonds formed between carboxyl and amino groups that are not involved in the formation of peptide bonds, they are weaker than disulphide bridges

48
Q

What are hydrogen bonds like?

A

They are numerous however they are weak and easily broken

49
Q

What is the bond between two amino acids?

A

A peptide bond

50
Q

How are peptide bonds formed?

A

The joining of amino acids by a condensation reaction