2.2 Proteins Flashcards

(50 cards)

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
What changes in the structure of amino acids?
The R group changes, but all amino acids have the same general structure
26
What are the four structures of proteins?
* primary structure * secondary structure * tertiary structure * quaternary structure
27
How many naturally occurring amino acids are there?
There are 20 naturally occurring amino acids each with their own R group
28
How is a polypeptide chain formed?
When amino acids are added to a dipeptide
29
How many polypeptides does one protein consist of?
One polypeptide
30
What is polymerisation? And what type of reaction is this?
The process in which amino acid monomers are joined to form a polypeptide, this is a condensation reaction
31
What are the types of proteins?
* structural * catalytic * signalling * immunological
32
What are structural proteins?
They are the main component of body tissues such as muscle, skin, hair and ligaments
33
What are catalytic enzymes?
All enzymes are proteins catalysing many biochemical reactions
34
What are signalling proteins?
Hormones and receptors (many of these are proteins)
35
What are immunological proteins?
Antibodies are proteins
36
Where is a disulphide bridge formed?
Between two cystine amino acids
37
What does the primary protein structure look like? And what bond joined them?
A long chain of amino acids joined by polypeptide bonds
38
What doe the primary structure of a protein determine?
It's shape and function
39
What are the two secondary structures?
* alpha helix | * beta pleated sheet
40
What bond does the secondary structure contain?
Weak hydrogen bonds
41
How are the weak hydrogen bonds form?
The positive charge on the hydrogen and the negative charge of the oxygen
42
What do the hydrogen bonds cause in the secondary structure?
Causes the long polypeptide chains to twist into a 3D helix
43
What is the tertiary structure?
The 3rd protein structure it is a further folded and twisted to give it a more complex 3D structure
44
How is the tertiary structure maintained?
By a number of bonds
45
What bonds are contained in the tertiary structure?
* disulphide bonds * ionic bonds * hydrogen bonds
46
What are disulphide bonds?
Bridges formed between cystine they are strong and difficult to break
47
What are ionic bonds?
Bonds formed between carboxyl and amino groups that are not involved in the formation of peptide bonds, they are weaker than disulphide bridges
48
What are hydrogen bonds like?
They are numerous however they are weak and easily broken
49
What is the bond between two amino acids?
A peptide bond
50
How are peptide bonds formed?
The joining of amino acids by a condensation reaction