Proteins Flashcards

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1
Q

What are the monomers of proteins?

A

Amino acids

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2
Q

What are polymers of amino acids?

A

Polypeptides

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3
Q

What is the protein that plays a structural role in hair?

A

Keratin

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4
Q

What is the protein that plays a structural role in clotting?

A

Fibrin

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5
Q

What gives proteins a structural function?

A

Their rigid structure

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6
Q

What are enzymes?

A

Biological catalysts that accelerate chemical reactions

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7
Q

What is essential for protein structure?

A

3D shape

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8
Q

What must be correct for the correct structure?

A

Protein transcript

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9
Q

How does a transport protein work?

A

Large molecules pass through the membrane through active transport which causes the protein to flip

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10
Q

What is a channel protein?

A

Specific ions bind to receptors and the molecule is allowed through

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11
Q

What do membrane proteins allow?

A

Transport of polar substances through the phospholipid bilayer through diffusion and active transport

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12
Q

What transports iron in the body?

A

Transferrin

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13
Q

What transports oxygen around the body?

A

Haemoglobin

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14
Q

What transports oxygen to muscles?

A

Myoglobin

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15
Q

What shape protein is essential for transport?

A

Globular

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16
Q

What type of protein is part of the immune system?

A

Antibodies

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17
Q

How do antibodies function?

A

They recognise foreign substances and induce an immune response

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18
Q

How do muscles contract?

A

The sliding action between filaments of actin & myosin

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19
Q

An example of a protein that contracts in the digestive tract?

A

Cilia

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20
Q

An example of a protein that contracts during mitosis?

A

Spindle fibres

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21
Q

What proteins are intercellular messengers?

A

Hormones

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22
Q

What do hormones do?

A

Influence the metabolism of cells

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23
Q

How does insulin enter cells?

A

Receptor protein reacts with insulin & opens channel proteins for glucose to enter cells

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24
Q

Name an enzyme involved in the glycolytic pathway

A

Glycogen synthase

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25
Q

Name an enzyme involved in DNA replication

A

DNA polymerase

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26
Q

Name an enzyme that allows lactose to cross cell membrane

A

Lactose permease

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27
Q

Name a structural protein found in connective tissue

A

Collagen

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28
Q

Name 3 proteins involved in the immune system

A

Antibodies, cytokines & chemokines

29
Q

Name 3 parts of an amino acid attached to the planar carbon

A

Amino group, R side chain & carboxyl group

30
Q

What is the only difference between amino acids

A

The R side chain

31
Q

What does the R side chain influence?

A

How the protein folds & its 3D structure

32
Q

How many distinct amino acids are there?

A

20

33
Q

Name 2 subdivisions of amino acids

A

Hydrophobic and Hydrophilic

34
Q

Name some characteristics of hydrophobic amino acids

A

Repel aqueous solution, reside on the interior of proteins, doesn’t ionise or form hydrogen bonds

35
Q

Name some characteristics of hydrophilic amino acids

A

Interact with aqueous solution, reside on the exterior of proteins, form hydrogen bonds

36
Q

What is physiological pH?

A

7.4

37
Q

What charge does an amino acid have at physiological pH?

A

No charge

38
Q

What name is given to the neutral charged amino acid molecule at physiological pH?

A

Zwitterion

39
Q

What is the carboxyl group (COOH) converted to at physiological pH?

A

COO-

40
Q

What is the amine group (NH2) converted to at physiological pH?

A

NH3+

41
Q

Which of the groups of an amino acid is acidic?

A

The carboxyl group

42
Q

Which of the groups of an amino acid is basic?

A

The amino group

43
Q

What happens if you increase the pH of an amino acid solution?

A

A proton from the amino group will bond with a hydroxide ion to form water molecules and the amino acid is given a negative charge

44
Q

What happens if you decrease the pH of an amino acid solution?

A

A proton will bond with the carboxyl group and the molecule will be given a positive charge

45
Q

When the net charge of an amino acid is 0, the pH is said to be…

A

Isoelectric point (pI)

46
Q

Non-polar aliphatic amino acids

A

Glycine, alanine, valine, leucine, methionine, isoleucine

47
Q

Polar & uncharged amino acids

A

Serine, threonine, cysteine, proline, asparagine, glutamine

48
Q

Aromatic amino acids

A

Phenylalanine, tyrosine, tryptophan

49
Q

Positively charged amino acids

A

Lysine, arginine, histidine

50
Q

Negatively charged

A

Aspartate, glutamate

51
Q

What is primary structure?

A

Specific sequence of amino acids joined by peptide bonds

52
Q

What is the free amino group called in the primary structure?

A

N terminus

53
Q

What is the free carboxyl group called in the primary structure?

A

C terminus

54
Q

What is secondary structure?

A

Local foldings of chains of amino acids

55
Q

Name the 2 types of secondary structure

A

Alpha helix & beta pleated sheets

56
Q

What holds the secondary structure in place?

A

Hydrogen bonds

57
Q

What atoms form hydrogen bonds with each other during secondary structure?

A

The carbonyl O and an amino H

58
Q

What bonding pattern causes the alpha helix structure?

A

The carbonyl O in the backbone bonds with the H of an amino group 4 amino acids down

59
Q

What type of bonding causes beta pleated sheets?

A

When a peptide chain turns back on itself or if 2 chains line up close to each other

60
Q

What is tertiary structure?

A

The 3D structure of a protein

61
Q

Do all proteins have quaternary structure?

A

No

62
Q

What is quaternary structure?

A

Polypeptides join together

63
Q

How many peptide chains in haemoglobin?

A

4

64
Q

How many peptide chains in DNA polymerase?

A

10

65
Q

What is denaturation?

A

Protein loses its higher order structure but not primary structure

66
Q

What causes denaturation?

A

Inappropriate heat, pH, and chemical reactions

67
Q

What is the name given to a denatured protein that regains its shape

A

Renatured

68
Q

What type of reaction forms peptide bonds?

A

Condensation dehydration

69
Q

What molecule is lost in a condensation dehydration reaction?

A

Water