3.1.4 Proteins 3.1.4.1 General Properties Of Proteins Flashcards

1
Q

3 examples of proteins that are vital compounds of all living organisms

A

Enzymes
Antibodies
Hormones

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2
Q

3 functions of proteins in the body e.g

A

Holding body together
Controlling body chemistry (metabolism)
Fighting off disease (immune response)

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3
Q

What element do organic molecules contain

A

Carbon

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4
Q

What type of molecules are proteins

What 4 elements do they always contain

A

Large, complex molecules

Carbon, hydrogen, oxygen, nitrogen

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5
Q

What’s nitrogen in proteins for

A

Growth

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6
Q

What do mostly primary + secondary proteins sometimes contain

A

Sulphur

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7
Q

What are the monomers that make up proteins

A

Amino acids

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8
Q

What do amino acids mostly all end in

E.g

A

‘-ine’

Proline, valine

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9
Q

2 words that link with nitrogen

A

Amino
Amine
Amide

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10
Q

2 parts of an amino acid that always stay the same

A

Amino group

Acid group

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11
Q

What’s the formula of the amino group

A

NH2

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12
Q

What’s the formula of the acid group

A

COOH

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13
Q

What part of an amino acid is always different

A

The R group

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14
Q

How many different amino acids are there and so different r groups

E.g

A

20

E.g glycine, alanine

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15
Q

Where is sulphur found if it’s present in an amino acid

A

The R group

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16
Q

What’s the test for proteins

A

The Biuret Test

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17
Q

What do you not need for the test for proteins

A

Heat

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18
Q

What’s the method for the biuret test

A

Dissolve test substance in water (crush it if it’s a seed or really solid food)
Add biuret reagent

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19
Q

What’s the biuret reagent consist of

A

Copper sulfate + sodium hydroxide mixture

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20
Q

What shows protein is present at the end of the biuret test

A

Change in colour from blue to lilac/purple

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21
Q

What dl enzymes do in the body

A

The controlling

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22
Q

How are enzymes made

E.g

A

By adding ‘-ase’ to the substrate

E.g
Lactase breaks down lactose

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23
Q

2 types of enzymes

A
Intracellular (working inside cells)
Extra cellular (working outside cells) - fungi
24
Q

How do amino acids join
What bonds are formed between them
Whats released

A

By condensation reactions
Releasing water
Forming peptide bonds

25
How many amino acids In a dipeptide
2
26
How many amino acids In a tripeptide
3
27
How many amino acids In a polypeptide
Many
28
Whats protein made from (not amino acids) E.g
1/more polypeptides (polymers) E.g haemoglobin molecule made from 4 polypeptides (2 alpha + 2 beta polypeptide chains)
29
What has the backbone N-C-C-N-C-C
Dipeptide
30
How many levels of structure do proteins have
4
31
What's the first structure called | What is it
Primary structure | The sequence of amino acids (order in which they are joined)
32
3 words describing the primary structure
Long, fibrous strands
33
What type of proteins are primary and secondary structure
Structural
34
What's the 2nd level of proteins structure | What's the amino acid chain like now
Secondary structure | Folded and coiled
35
What's the secondary structure held in place by
Hydrogen bonds
36
2 most common secondary structure proteins
Alpha helix-spiral shape | Beta sheet - pleated like folded paper e.g silk from worms
37
What's the 3rd level of protein structure called | What's it like
Tertiary structure | Overall shape of amino acid chain (globular) e.g whole polypeptide
38
How does the tertiary structure become globular
When in water e.g cytoplasm , a wide variety of forces combine to twist, fold and bend the polypeptide into its most stable shape
39
What are there many areas of in the tertiary structure
Secondary structure
40
What type of proteins are the 3rd and 4th structural level
Functional
41
What's the 4th structural protein level called When does it occur E.g
Quaternary structure When the protein has more than 1 polypeptide chain E.g haemoglobin has 4
42
What structure does a protein made up of just 1 polypeptide chain not have
Quaternary
43
What component do quaternary proteins often have E.g
A non-protein component which is sometimes an ion E.g the haem in haemoglobin
44
What group is the haem in haemoglobin know as
Prosthetic group
45
What are the 2 main groups protein structure can be split into
Globular | Fibrous
46
What type of protein is globular
Functional - tertiary
47
What type of protein is fibrous
Structural - secondary
48
2 facts about globular proteins
Generally rounded in shape | Tend to have a chemical function
49
4 examples of chemical functions globular proteins may have What are these all
``` Enzymes Hormones e.g insulin Haemoglobin Antibodies Membrane proteins ``` All shape-specific
50
2 facts about fibrous proteins
Usually long,thin molecules | Generally have a structural function
51
What are fibrous proteins the fabric of
The body
52
3 examples of fibrous proteins and their uses
Collagen - strength to tissues Keratin - strength to skin, hair, nails Actin + myosin - muscles contract
53
What 2 relatively weak forces is the shape of globular proteins maintained by
Hydrogen bonds | Ionic bonds
54
Where do the hydrogen bonds and ionic bonds in globular proteins come from
The acidic and amine groups
55
What forces to big, tough fibrous proteins rely more on
Strong disulfide bridges