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Science For Medicine > Proteins > Flashcards

Proteins Flashcards

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1
Q

What is the step called which copies a genes DNA sequence to make an RNA molecule?

A

Transcription

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2
Q

What is the step called whereby an RNA molecule is coded into a protein?

A

Translation

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3
Q

What is an amino acid made up of?

A

An amino group, a carboxylic acid group and a side chain

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4
Q

What is primary protein structure?

A

The sequence of amino acids in a polypeptide chain

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5
Q

Where and when do peptide bonds form?

A

Within a ribosome during translation

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6
Q

What is secondary protein structure?

A

The spatial arrangement of amino acid residues that are near each other in the linear sequence

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7
Q

Where are examples of secondary structure found?

A

Alpha helices (in myoglobin/ferritin) and beta pleated sheets (fatty acid binding protein/porin)

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8
Q

What is the beta pleated sheet held together by?

A

Hydrogen bonds between amid groups of linear polypeptide chains

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9
Q

What is tertiary protein structure?

A

The spatial arrangement of amino acid residues that are far apart in a linear sequence

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10
Q

What kind of forces can hold amino acids together in the tertiary structure?

A

van der Waals, ionic interactions, hydrogen bonds, disulphide bridges, hydrophobic interactions

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11
Q

Where do ionic interactions occur?

A

Occur between two close oppositely charged R groups, are strong

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12
Q

What are Van der Waals forces?

A

Non-specific, weak attractions between atoms, strong when large no of them exist

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13
Q

When do hydrogen bonds occur?

A

When H is bonded to either O, N or F and a lone pair of electrons are present

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14
Q

What is the difference between Van der Waals and hydrogen bonds?

A

Hydrogen bonds are stronger and permanent

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15
Q

What are hydrophobic interactions?

A

Intra-polypeptide interactions which occur in an environment within proteins from which water is excluded

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16
Q

What are disulphide bridges?

A

Strong covalent bonds between two cysteine residues

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17
Q

When can disulphide bonds occur?

A

Common in extra-cellular proteins and can occur between, as well as, within a polypeptide

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18
Q

What is quarternary protein structure?

A

The spatial arrangement of individual polypeptide chains in a multi-subunit protein

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19
Q

What structures are disruption or destroyed during protein denaturation?

A

Both secondary and teritary structures

20
Q

Why does the primary structure remain the same after a denaturation process?

A

Denaturation reactions not strong enough to break peptide bonds

21
Q

What are some causes of denaturation of proteins?

A

Acids, heat, solvents

22
Q

What are the effects of denaturation?

A

Decreased solubility, altered water binding capacity, loss of biological activity, improved digestibility

23
Q

What enzymes cleave peptide bonds?

A

Peptidases

24
Q

What enzymes cleave internal bonds?

A

Endopeptidases

25
Q

What enzymes cleave one amino acid at a time?

A

Exopeptidases

26
Q

What enzymes cleave from the -COOH terminal?

A

Carboxypeptidases

27
Q

What enzymes cleave from the -NH2 terminal?

A

Aminopeptidases

28
Q

What are glycoproteins composed of?

A

Protein and carbohydrate

29
Q

What is an example of a glycoprotein?

A

Immunoglobulins

30
Q

Where does glycosylation occur?

A

In the ER and Golgi apparatus

31
Q

What does glycosylation have roles in?

A

Protein stabilisation, affects solublity, protein orientation, signalling and cell recognition

32
Q

How are glycoproteins formed?

A

Glycosylation whereby sugar molecule binds via amino acid to the protein

33
Q

What are lipoproteins?

A

Protein and lipids which are either covalently or non-covalently bonded together

34
Q

What is the function of lipoproteins?

A

Transport of water-insoluble fats and cholesterol in the body

35
Q

What is a metalloprotein?

A

A protein molecule with a bound metal ion

36
Q

What functions can a metalloprotein help with?

A

Enzymes, storage, signalling, transport

37
Q

How does haemoglobin transport O2?

A

Haem group at centre of each polypeptide chain binds one molecule of oxygen

38
Q

How many molecules of oxygen can one haemoglobin molecule bind?

A

Four

39
Q

What kind of binding means that a haemoglobin molecules takes not one, but four oxygens?

A

Co-operative binding

40
Q

Why does scurvy happen in relation to collagen?

A

Vitamin C needd to convert proline to hydroxyproline which is essential for stabilising crosslinks between chains and so a weaker collagen is produced

41
Q

What structures are lost with osteogenesis imperfecta?

A

Secondary and tertiary structures

42
Q

Why is a weaker and brittle collagen produced with osteogenesis imperfecta?

A

Glycine substituted, protein can no longer fold to form tight coil, reduced interacton between fibrils, loss of structure

43
Q

What happens when LDL receptor mutation?

A

Different possible effectors: no receptors, receptors can’t bind LDL, receptors don’t release LDL

44
Q

What kind of genetic disorder is Familial Hypercholesterolemia?

A

Autosomal dominant

45
Q

What causes Familial Hypercholesterolemia?

A

Mutation in LDL receptor gene meaning elevated LDL conc in blood

46
Q

What are effects of Familial Hypercholesterolemia?

A

Cholesterol deposition in skin, tendons and arteries and a risk of early CVD

Science For Medicine (7 decks)

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