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Biology Module 2 > Proteins 2.1.2 (k,l,m,n,o) > Flashcards

Proteins 2.1.2 (k,l,m,n,o) Flashcards

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1
Q

monomer of a protein?

A

amino acids

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2
Q

what is formed with two amino acids?

A

a dipeptide

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3
Q

what is an amino acid chain?

A

a polypeptide

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4
Q

what is the general structure of an amino acid?

A
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5
Q

what bonds link amino acids together?

A

peptide bonds

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6
Q

what reaction forms peptide bonds?

A

condensations

a molecule of water is produced

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7
Q

what reaction destroys peptide bonds?

A

hydrolysis

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8
Q

what are the levels to protein structure?

A

primary
secondary
tertiary
quaternary

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9
Q

what is the primary structure of a protein?

A

the sequence of amino acids in a polypeptide chain

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10
Q

what bonds are present in the primary structure?

A

peptide bonds

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11
Q

what is the secondary structure of a protein?

A

the coiling of the polypeptide chain into:
- alpha helix
- beta pleated sheet

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12
Q

alpha helix

A
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13
Q

beta-pleated sheet

A
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14
Q

what bonds are present in the secondary structure?

A

peptide bonds
hydrogen bonds

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15
Q

what is the tertiary structure of a protein?

A

the further folding of a polypeptide chain into it’s 3D structure

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16
Q

what bonds are present in the tertiary structure?

A

ionic
disulfide bridges
hydrophobic-hydrophilic interactions
hydrogen bonds

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17
Q

in the tertiary structure what are the bonds formed between?

A

the R-groups of a protein

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18
Q

ionic bonding

A

between oppositely charged R-groups

19
Q

disulfide bridges

A

between two R-groups which both contain cysteine

20
Q

hydrophobic-hydrophilic interactions

A

between hydrophobic and hydrophilic R-groups

21
Q

hydrogen bonds

A

between delta +ve and delta -ve R -groups

22
Q

what is the quarternary structure?

A

the interactions between more than one polypeptide chain

the final 3D structure

23
Q

what are the two types of protein?

A

globular
fibrous

24
Q

properties of globular proteins

A

compact
spherical
water soluble

25
Q

how are globular proteins water soluble?

A

they have their hydrophobic R-groups pointing inwards
they have their hydrophilic R-groups pointing outwards

26
Q

why is water solubility important for globular proteins?

A

they have to be able to be dissolved in water to be transported

27
Q

examples of globular proteins

A

insulin
haemoglobin
catalase

28
Q

role of insulin

A

hormone which decreases the blood glucose level

29
Q

structure of insulin

A

two polypeptide chains
joined together by disulfide bridges

30
Q

what is a conjugated protein?

A

a protein which contains a non-protein element called a prosthetic group

31
Q

example of a conjugated protein

A

haemoglobin

32
Q

what is the prosthetic group in haemoglobin?

A

Fe2+

33
Q

structure of haemoglobin

A

4 polypeptides
with 2 alpha and 2 beta subunits

each subunit contains a prosthetic group of Fe2+

34
Q

what does the Fe2+ do?

A

binds to oxygen or carbon dioxide which allows haemoglobin to transport it around the body

35
Q

why does haemoglobin have to be water soluble?

A

it needs to be able to dissolve in the blood to be transported around the body

36
Q

role of catalase

A

breaks down hydrogen peroxide

37
Q

structure of catalase

A

four prosthetic groups
each have their own haem grou[

38
Q

properties of fibrous proteins

A

long
insoluble
strong - high tensile strength

39
Q

properties of fibrous proteins

A

long
insoluble
strong - high tensile strength

40
Q

examples of fibrous proteins

A

collagen
keratin
elastin

41
Q

properties of collagen

A

strong
flexible
insoluble

42
Q

what makes collagen strong?

A

presence of cysteine means that disulfide bridges are formed which require a lot of energy to overcome

43
Q

properties of elastin

A

flexible

Biology Module 2 (30 decks)

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