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Cfe Advanced Higher Biology > Unit 1 - Cells and Proteins > Flashcards

Unit 1 - Cells and Proteins Flashcards

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1
Q

What is the proteome?

A

The entire set of proteins expressed by a genome

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2
Q

What makes the proteome larger that the genome?

A

Post-translational modification and alternative/RNA splicing

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3
Q

What is alternative/RNA splicing?

A

The joining of exons after introns are removed from the primary transcript

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4
Q

What are introns?

A

Non-coding regions of mRNA

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5
Q

What is post-translational modification?

A

Changes made to polypeptides following translation

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6
Q

Examples of post-translational modification.

A

Cutting the polypeptide chain and reassemble a modified version (insulin by cleavage (cutting) of proinsulin), add a functional group such as a carbohydrate or phosphate group (add carbohydrate to make glycoprotein)

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7
Q

What are the distinguishing features of protein molecules?

A

Folded nature, ability to bind tightly and specifically to other molecules (ligands)

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8
Q

Binding sites on the protein are complementary to the…

A

ligand

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9
Q

What does the ligand binding do to the protein?

A

Causes a conformational change

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10
Q

What does a conformational change do to the protein?

A

It can result in an altered function

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11
Q

What do all amino acids have?

A

A central carbon with four groups attached (an amine (NH2)), a carboxylic acid (COOH), a hydrogen and a variable R group

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12
Q

What does the R group on a protein do?

A

Determines the amino acids characteristics

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13
Q

Hydrophilic molecules are…

A

Polar

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14
Q

Hydrophobic molecules are…

A

Non polar

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15
Q

R groups that are positively charged are…

A

Basic

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16
Q

R groups that are negatively charged are…

A

Acidic

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17
Q

What’s the key component of a negatively charged, hydrophilic amino acid?

A

Carboxylic acid group

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18
Q

What’s the key component of a positively charged, hydrophilic amino acid?

A

Amine group

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19
Q

What’s the key component of a polar, hydrophilic amino acid?

A

Carbonyl, hyrdoxyl, amine groups

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20
Q

What’s the key component of a non-polar, hydrophobic amino acid?

A

Hydrocarbon group

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21
Q

What are the four levels of protein structure?

A

Primary, secondary, tertiary, quaternary

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22
Q

What is the primary structure of a protein?

A

The linear sequence of amino acids

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23
Q

Example of primary structure.

A

Insulin, shapes to bind to receptor proteins in the plasma membrane of liver muscle and fat cells

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24
Q

What is the secondary structure of a protein?

A

a-helix (alpha helix) and b-pleated (beta pleated) sheets are formed by hydrogen bonding

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25
Q

What type of bonding is it and where on the protein is it on secondary structure?

A

Hydrogen, backbone of the protein

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26
Q

The bond in a-helices form between what two chemicals?

A

N-H and C=O groups

27
Q

What are the two varieties of beta-pleated sheets?

A

Parallel and antiparallel

28
Q

What is the tertiary structure of a protein?

A

Final 3D shape of protein fored by interactions between R-groups

29
Q

What is the difference between hydrophobic and hydrophilic amino acids in tertiary structure?

A

Hydrophobic cluster together in the interior of the protien. Hydrophilic predominate at the surface of the protein

30
Q

What bonds are involved on tertiary structure?

A

Ionic (atoms are oppositely charged) , hydrogen and disulphide (covalent bond between two thiol groups) bonds

31
Q

What is Van der Waals interaction?

A

Caused by fluctuations in elecron clouds around molecules which cause them to become slightly positively or negatively charged. May result in attraction or repulsion between atoms

32
Q

What are prosthetic groups?

A

Non-protein parts

33
Q

What do prosthetic groups do?

A

Give proteins added function e.g. haem in myoglobin

34
Q

What is quaternary structure?

A

Several connected polypeptide subunits which are linked by bonds between R groups of the polypeptide chain

35
Q

Give an example of quaternary structure.

A

Haemoglobin

36
Q

What influences the interactions of the R groups?

A

pH and temperature

37
Q

What’s the difference between integral and peripheral proteins?

A

Integral proteins are held within the membrane, peripheral proteins are loosely associated with the plasma membrane

38
Q

What does it mean if some integral proteins are transmembrane?

A

They span the entire width of the membrane

39
Q

Examples of transmembrane proteins.

A

Channels, transporters and receptors

40
Q

What is a ligand?

A

A substance that can bind to a protein

41
Q

What does the fluid mosaic model describe?

A

The structure of the plasma membrane

42
Q

What are membranes comprised of?

A

A phospholipid bilayer and a patchwork of protein molecules

43
Q

What are histones?

A

Packing proteins that DNA wraps around

44
Q

How are nucleosomes formed?

A

When DNA is wrapped around histones

45
Q

What are activator proteins?

A

They bind to specific DNA sequences and stimulate transcription

46
Q

What is needed to allow a reaction to occur?

A

Activation energy

47
Q

What happens to a reaction (the activation energy) when a catalyst is present?

A

The activation energy is lowered

48
Q

In living systems, how do enzymes lower the activation energy?

A

By forming an enzyme-substrate complex

49
Q

Describe induced fit in enzymes.

A

When the correct substrate binds to the enzyme a temporary change in the conformation occurs increasing the binding and interaction (affinity) with the substrate

50
Q

What is an allosteric enzyme?

A

One which changes conformation upon binding a modulator

51
Q

Where do modulators bind on an allosteric enzyme?

A

Secondary sites called allosteric sites

52
Q

What do negative modulators do?

A

Reduce the enzyme’s affinity for the substrate

53
Q

What do positive modulators do?

A

Increase the enzyme;s affinity for the substrate

54
Q

How does haemoglobin show cooperativity?

A

When each polypeptide subunit (containing a haem group capable of binding to oxygen) the next one binds more easily and more easily. This is positive cooperativity.

55
Q

What does the cooperative binding of O2 with haemoglobin do?

A

It allows blood to carry about 60 times more O2 than it could if O2 dissolved in the plasma

56
Q

What happens to the saturation of oxyhaemoglobin when the temperture is decreased and the pH is increased?

A

It increases

57
Q

What happens to the saturation of oxyhaemoglobin when the temperture is increased and the pH is decreased?

A

It decreases

58
Q

What factors affect haemoglobin’s ability to bind to oxygen?

A

Temperature and pH

59
Q

What do kinase enzymes do?

A

Responsible for the phosphorylation of other proteins

60
Q

What do phosphatase enzymes do?

A

Catalyse dephosphorylation

61
Q

What does the addition or removal of phosphate from particular R groups cause?

A

Reversible conformational changes in proteins

62
Q

What is a sarcomere?

A

A basic unit of muscle

63
Q

What proteins are in a sarcomere?

A

Actin and myosin

64
Q

What happens during muscle contraction?

A

Myosin have heads that act as cross bridges as they bind to actin. When ATP binds to myosin, the myosin head detaches from actin, swings forward and rebinds. The rebinding releases the ADP and a phosphate and drags the myosin along the actin filament (power stroke)

Cfe Advanced Higher Biology (4 decks)

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