PROTEINS Flashcards

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
When are disulfide bridges formed
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
Are disulfide bridges strong and what does this mean
yes, they cannot be easily broken
27
What is the quaternary structure of proteins
the way that different polypeptide chains in a protein are held together
28
What is the final structure of a single polypeptide chain protein
teritary
29
Give an example of a quaternary structure protein
haemoglobin
30
What 4 functions do proteins have
1) enzymes 2) antibodies 3) transport proteins 4) structural proteins
31
What shape are enzymes usually and why
spherical due to the tight folding of the polypeptide chains
32
What do enzymes often have roles in
metabolism or synthesis
33
Are enzymes soluble
yes
34
What are antibodies used in
immune response
35
What are antibodies make up of
2 light (short) and 2 heavy (long) polypeptide chains bonded together
36
What regions do antibodies have and what varies within them
variable regions, the amino acid sequences vary
37
What is another name for transport proteins
channel proteins
38
Where are transport proteins found
cell membrane
39
What causes the channel proteins to fold up and form a channel
they contain hydrophobic and hydrophilic amino acids
40
What do these transport proteins transport
molecules and ions across membranes
41
What do structural proteins consist of
long polypeptide chains lying parallel to each other with cross-links between them
42
Give 2 examples of structural proteins
keratin (hair), collagen (connective tissue)
43
Are structural proteins strong
yes
44
What test is used for proteins
Biuret test
45
How many steps are there in the Biuret test
3
46
What are the steps for the Biuret test
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
What indicates the presence of lipids
a colour change from blue to purple
48
What are the 2 types of protein
fibrous and globular
49
What functions do fibrous proteins have
structural
50
What functions do globular proteins have
metabolic
51
Give an example of a fibrous protein
collagen
52
What is the primary structure of collagen
unbranches polypeptide chain
53
What is the secondary structure of collagen
very tightly wound
54
What helps the secondary structure be very tightly wound
lots of the amino acid glycine
55
What is the tertiary structure of collagen
chain is twisted into a second helix
56
What is the quaternary structure of collagen
3 polypeptide chains wound together (like that of a rope)
57
Where is collagen found
in tendons