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Snazzy Skeleton > Biological molecules p57-65 > Flashcards

Biological molecules p57-65 Flashcards

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1
Q

What are all proteins made up of?

A

amino acids

one or more polypeptide chains

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2
Q

Give two examples of proteins in the blood.

A
  • some hormones such as insulin and glucagon
  • oxygen-carrying pigment such as haemoglobin and myoglobin
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3
Q

Which proteins are for muscle contraction?

A

actin and myosin

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4
Q

What are examples of storage products made of protein?

A

ovalbumin in egg
casein in milk

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5
Q

Name 5 examples of proteins.

A

enzymes, transport proteins, antibodies, collagen (bones, artery wall), keratin (hair, nails and surface layer of skin)

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6
Q

What do amino acids consist of?

A

amino group -NH2
carboxylic acid group -COOH
carbon and hydrogen atom
R group (eg: hydrogen atom)

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7
Q

Different amino acids have different…

A

R groups

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8
Q

Two amino acids linked together is

A

a dipeptide

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9
Q

Many amino acids linked together is

A

a polypeptide

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10
Q

Explain the peptide bond between two amino acids.

A

The -HO of the carboxylic acid group of one amino acid. The H of the second amino acid.

C of first bonds with N of second.

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11
Q

Where is protein digested?

A

stomach and the small intestine

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12
Q

Primary structure

A

which amino acids in which specific sequence

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13
Q

How does the change in a single amino acid (even if there are thousands), affect a protein/polypeptide?

A

properties changed

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14
Q

Secondary structure

A

structure of a protein resulting from coiling/folding

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15
Q

What enables non-adjacent amino acids to affect each other?

A

Polypeptide chain bends back on itself

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16
Q

How are alpha helixes coiled into a firm structure?

A

Held together by hydrogen bonds due to polar characteristics of groups.

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17
Q

Explain hydrogen bonding for an alpha helix.

A

O of C=O of one.
H of -NH of toher, 4 places ahead

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18
Q

How is a beta pleated sheet held together

A

hydrogen bonding

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19
Q

Describe the shape of a beta pleated sheet.

A

looser, straighter shape

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20
Q

What are the hydrogen bonds holding the alpha-helixes and beta-pleated sheets together, easily broken by?

A

high temperature
pH changes

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21
Q

What does the arrangement of proteins depend on?

A

The R groups present.
Attractions between amino acids.

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22
Q

Tertiary structure

A

a folded/coiled secondary structure

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23
Q

Name the four bonds which keep folded proteins in their precise shapes.

A

Hydrogen bond
Hydrophobic interactions
Ionic bond
Disulfide bond

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24
Q

Hydrogen bond

A

Hydrogen bonds form between a variety of R groups. Happens between strongly polar groups.

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25
Q

Ionic bond

A

Ionic bonds form between R groups containing ionised amino and ionised carboxyl groups. Broken down by pH changes.

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26
Q

Disulfide bond

A

The sulfur atoms of two neighbouring cysteine molecules join with a covalent bond. Broken down by reducing agents.

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27
Q

Hydrophobic interactions

A

Hydrophobic interactions happen between non-polar R groups. Shape of many proteins are affected by this. Weak, but strong together.

28
Q

Describe the behavior of hydrophobic and hydrophilic R groups in a watery environment.

A

Phobics come together, excluding water. They are at the centre, facing away from watery environment.

Philics surround phobics, facing outwards in contact with the watery environment.

29
Q

Quaternary structure

A

overall structure formed by polypeptide chains

30
Q

How many polypeptide chains does haemoglobin have?

A

4 chains

31
Q

Which type of stucture is haemoglobin?

A

quaternary

32
Q

How are quaternary structure held together?

A

By the same 4 bonds as in tertiary structures

33
Q

Give 3 examples of globular proteins.

A

haemoglobin, myoglobin, enzymes

34
Q

Describe the shape of globular proteins.

A

Protein whose molecules curl up into a ball

35
Q

Why do globular proteins usually curl up?

A

The phobic can point to molecule’s centre. Philic remain on the outside of molecule.

36
Q

Are globular proteins usually soluble or insoluble and why?

A

Soluble, because water molecules cluster around philic.

37
Q

Many globular proteins have a role in..

A

metabolic reactions

38
Q

Why do globular proteins have precise shapes?

A

For their functions.

39
Q

Are fibrous proteins usually soluble or insoluble?

A

not usually soluble

40
Q

What is the role of fibrous proteins?

A

Most have structural roles. Eg: keratin makes structure waterproof.

41
Q

Give two examples of fibrous proteins.

A

keratin and collagen

42
Q

Fibrous proteins form..

A

long strands

43
Q

What is each chain of a haemoglobin molecule?

A

A protein called globin, which is related to myoglobin, and so, has a similar tertiary structure.

44
Q

How many types of globin are there?

A

many

45
Q

Which globins are used to make haemoglobin?

A

alpha-globin and beta-globin

46
Q

What are the haemoglobin chains made of?

A

Two alpha chains made of alpha-globin, two beta chains made of beta-globin

47
Q

Describe the shape of a haemoglobin molecule.

A

nearly spherical

48
Q

What is important in holding the correct 3D shape of haemoglobin?

A

interactions between the phobic

49
Q

What happens in sickle cell anemia?

A

one amino acid on beta-chain surface is replaced with another

glutamic acid (polar) is replaced with valine (non-polar)

50
Q

What is the consequence of sickle cell anemia?

A

Haemoglobin molecule is less soluble

51
Q

What does each haemoglobin chain have?

A

haem group

52
Q

What is a haem group?

A

An important, permanent part of a protein molecule (not out of amino acids) is called a prosthetic group.

53
Q

What is the haem group responsible for?

A

Colour which depends on whether the iron atoms are combined with oxygen. Oxyhaemoglobin is bright red. Without O, darkish, blueish red.

54
Q

What does a haem group contain?

A

an iron atom to which an oxygen molecule can bind

55
Q

Is collagen globular or fibrous?
Soluble or insoluble?

A

insoluble and fibrous

56
Q

Role of collagen

A

structural role

57
Q

Describe collagen

A

flexible, high tensile strength

58
Q

Describe collagen’s structure.

A

Each chain is in the shape of a helix. Three chains. They wind around each other to form a triple helix. Held together by H and some covalent bonds.

59
Q

What is the most common protein?

A

collagen, making up 25% of protein in mammals

60
Q

Almost every third amino acid in each polypeptide of collagen is..

A

glycine, the smallest amino acid

61
Q

Where is glycine found in collagen?

A

Found on the inside of strands. Its small size allows the three strands to lie close together and form a tight coil.

62
Q

Parallel collagen molecules are cross-linked forming..

A

fibrils

63
Q

Many fibrils alongside each other, forms..

A

fibres

64
Q

How are parallel collagen molecules cross-linked?

A

Covalent bonds between Rgroups of amino acids lying next to each other.

65
Q

Many collagen molecules make up..

A

one collagen fibre

66
Q

How do the ends of the parallel collagen molecules look?

A

Staggard, to strengthen the structure

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