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Biology - biological molecules + cells > 3.1.4 Proteins 3.1.4.1 General Properties Of Proteins > Flashcards

3.1.4 Proteins 3.1.4.1 General Properties Of Proteins Flashcards

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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
Q

How many amino acids In a dipeptide

A

2

26
Q

How many amino acids In a tripeptide

A

3

27
Q

How many amino acids In a polypeptide

A

Many

28
Q

Whats protein made from (not amino acids)

E.g

A

1/more polypeptides (polymers)

E.g haemoglobin molecule made from 4 polypeptides (2 alpha + 2 beta polypeptide chains)

29
Q

What has the backbone N-C-C-N-C-C

A

Dipeptide

30
Q

How many levels of structure do proteins have

A

4

31
Q

What’s the first structure called

What is it

A

Primary structure

The sequence of amino acids (order in which they are joined)

32
Q

3 words describing the primary structure

A

Long, fibrous strands

33
Q

What type of proteins are primary and secondary structure

A

Structural

34
Q

What’s the 2nd level of proteins structure

What’s the amino acid chain like now

A

Secondary structure

Folded and coiled

35
Q

What’s the secondary structure held in place by

A

Hydrogen bonds

36
Q

2 most common secondary structure proteins

A

Alpha helix-spiral shape

Beta sheet - pleated like folded paper e.g silk from worms

37
Q

What’s the 3rd level of protein structure called

What’s it like

A

Tertiary structure

Overall shape of amino acid chain (globular) e.g whole polypeptide

38
Q

How does the tertiary structure become globular

A

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
Q

What are there many areas of in the tertiary structure

A

Secondary structure

40
Q

What type of proteins are the 3rd and 4th structural level

A

Functional

41
Q

What’s the 4th structural protein level called
When does it occur

E.g

A

Quaternary structure
When the protein has more than 1 polypeptide chain

E.g haemoglobin has 4

42
Q

What structure does a protein made up of just 1 polypeptide chain not have

A

Quaternary

43
Q

What component do quaternary proteins often have

E.g

A

A non-protein component which is sometimes an ion

E.g the haem in haemoglobin

44
Q

What group is the haem in haemoglobin know as

A

Prosthetic group

45
Q

What are the 2 main groups protein structure can be split into

A

Globular

Fibrous

46
Q

What type of protein is globular

A

Functional - tertiary

47
Q

What type of protein is fibrous

A

Structural - secondary

48
Q

2 facts about globular proteins

A

Generally rounded in shape

Tend to have a chemical function

49
Q

4 examples of chemical functions globular proteins may have

What are these all

A 
Enzymes
Hormones e.g insulin
Haemoglobin 
Antibodies
Membrane proteins

All shape-specific

50
Q

2 facts about fibrous proteins

A

Usually long,thin molecules

Generally have a structural function

51
Q

What are fibrous proteins the fabric of

A

The body

52
Q

3 examples of fibrous proteins and their uses

A

Collagen - strength to tissues
Keratin - strength to skin, hair, nails
Actin + myosin - muscles contract

53
Q

What 2 relatively weak forces is the shape of globular proteins maintained by

A

Hydrogen bonds

Ionic bonds

54
Q

Where do the hydrogen bonds and ionic bonds in globular proteins come from

A

The acidic and amine groups

55
Q

What forces to big, tough fibrous proteins rely more on

A

Strong disulfide bridges

Biology - biological molecules + cells (16 decks)

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