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BIOLOGY - BIOLOGICAL MOLECULES > PROTEINS > Flashcards

PROTEINS Flashcards

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1
Q

What are amino acids

A

the basic monomer unit that combine to make the polymer polypeptide

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2
Q

What are the monomers of polypeptides

A

amino acids

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3
Q

What are proteins make up of

A

1 or more polypeptides

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4
Q

How many amino acids need to join to become a polypeptide

A

more than 2

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5
Q

What is formed if 2 amino acids join

A

dipeptide

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6
Q

What is the basic structure of amino acid

A

carbon atom attached to 4 chemical groups:

1) amine/ amino group (NH2)
2) carboxyl group (COOH)
3) hydrogen atom (H)
4) R group - variable (each amino acid has a different R group)

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7
Q

How many amino acids do living things share

A

20

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8
Q

What is the only amino acid that doesn’t have carbon in its side group

A

glycine

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9
Q

Draw the basic structure of an amino acid

A

C attatched to R, COOH, H, H2N

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10
Q

How are polypeptides formed

A

in a condensation reaction

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11
Q

How is water made in the condensation reaction of amino acids

A

the OH group from the carboxyl group of one amino acid joins to the H group from another amino acid

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12
Q

What bond is formed during the condensation reaction of amino acids and where is it formed between

A

peptide bond between carbon group of one amino acid and nitrogen atom of another

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13
Q

When are polypeptides hydrolysed

A

during digestion

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14
Q

What is polymerisation

A

the series of condensation reactions that joins many amino acid monomers together

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15
Q

What is the result of polymerisation

A

chain of hundreds of amino acids called a polypeptide

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16
Q

What is the sequence of amino acids in a polypeptide determined by

A

DNA

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17
Q

How many structural levels of proteins are there

A

4

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18
Q

What are the structural levels of proteins

A

1) Primary
2) secondary
3) tertiary
4) quaternary

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19
Q

What is the primary structure

A

the sequence of amino acids in a polypeptide chain

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20
Q

What does the primary structure determine

A

the polypeptide 3D shape and therefore its function

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21
Q

What can a change in the amino acid in the primary structure lead to

A

a change in shape of the protein and possibly stop it carrying out its function

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22
Q

What is the secondary structure of a protein

A

when the polypeptide chain has formed hydrogen bonds between the amino acids that cause it to change shape, into either an alpha helix or bea pleated sheet

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23
Q

Where are the hydrogen bonds formed between on the amino acids

A

The positive charge on the H of the NH group, and the negative charge on the O of the C=O group

24
Q

What is the tertiary structure of a protein

A

when the polypeptide chain is coiled further due to the creation of more bonds (hydrogen, ionic, disulfide bridges)

25
Q

When are disulfide bridges formed

A

when 2 molecules of the amino acid cysteine come close together and the sulfur atom in one cysteine bonds to the sulfur atom in the other

26
Q

Are disulfide bridges strong and what does this mean

A

yes, they cannot be easily broken

27
Q

What is the quaternary structure of proteins

A

the way that different polypeptide chains in a protein are held together

28
Q

What is the final structure of a single polypeptide chain protein

A

teritary

29
Q

Give an example of a quaternary structure protein

A

haemoglobin

30
Q

What 4 functions do proteins have

A

1) enzymes
2) antibodies
3) transport proteins
4) structural proteins

31
Q

What shape are enzymes usually and why

A

spherical due to the tight folding of the polypeptide chains

32
Q

What do enzymes often have roles in

A

metabolism or synthesis

33
Q

Are enzymes soluble

A

yes

34
Q

What are antibodies used in

A

immune response

35
Q

What are antibodies make up of

A

2 light (short) and 2 heavy (long) polypeptide chains bonded together

36
Q

What regions do antibodies have and what varies within them

A

variable regions, the amino acid sequences vary

37
Q

What is another name for transport proteins

A

channel proteins

38
Q

Where are transport proteins found

A

cell membrane

39
Q

What causes the channel proteins to fold up and form a channel

A

they contain hydrophobic and hydrophilic amino acids

40
Q

What do these transport proteins transport

A

molecules and ions across membranes

41
Q

What do structural proteins consist of

A

long polypeptide chains lying parallel to each other with cross-links between them

42
Q

Give 2 examples of structural proteins

A

keratin (hair), collagen (connective tissue)

43
Q

Are structural proteins strong

A

yes

44
Q

What test is used for proteins

A

Biuret test

45
Q

How many steps are there in the Biuret test

A

3

46
Q

What are the steps for the Biuret test

A

1) Place a sample of the solution into a test tube
2) add sodium hydroxide solution at room temperature to make the solution alkaline
3) Add very dilute sodium copper sulfate solution and mux

47
Q

What indicates the presence of lipids

A

a colour change from blue to purple

48
Q

What are the 2 types of protein

A

fibrous and globular

49
Q

What functions do fibrous proteins have

A

structural

50
Q

What functions do globular proteins have

A

metabolic

51
Q

Give an example of a fibrous protein

A

collagen

52
Q

What is the primary structure of collagen

A

unbranches polypeptide chain

53
Q

What is the secondary structure of collagen

A

very tightly wound

54
Q

What helps the secondary structure be very tightly wound

A

lots of the amino acid glycine

55
Q

What is the tertiary structure of collagen

A

chain is twisted into a second helix

56
Q

What is the quaternary structure of collagen

A

3 polypeptide chains wound together (like that of a rope)

57
Q

Where is collagen found

A

in tendons

BIOLOGY - BIOLOGICAL MOLECULES (12 decks)

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