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Veterinary Medicine > VETS-111 Cell Biology > Flashcards

VETS-111 Cell Biology Flashcards

0
Q

How is iron stored?

A

Complex with ferritin in the liver.

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1
Q

What is Transferrin?

A

Carries iron in blood plasma.

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2
Q

Functions of proteins

A

1) enzymology catalysts
2) transport and storage
3) movement
4) structural materials
5) immune protection antibodies
6) membranes
7) regulators and receptors

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3
Q

Structure of an amino acid in neutral solution

A

Zwitterion

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4
Q

Name if pH where amino acid has no net charge

A

Isoelectric

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5
Q

Two enantiomers of an amino acid

A

L and D-isomers

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6
Q

Which form of amino acids do proteins contain

A

L-isomer

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7
Q

Amino acids are joined by…

A

Peptide bonds

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8
Q

A polypeptide starts at which end?

A

Amino terminal residue

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9
Q

An amino acid ends at what end?

A

The carboxyl terminal residue

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10
Q

Is arginine an essential amino acid?

A

Yes

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11
Q

Is Histidine an essential amino acid?

A

Yes

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12
Q

Is Isoleucine an essential amino acid?

A

Yes

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13
Q

Is leucine an essential amino acid?

A

Yes

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14
Q

Is lycine an essential amino acid?

A

Yes

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15
Q

Is methionine an essential amino acid?

A

Yes

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16
Q

Is phenylalanine an essential amino acid?

A

Yes

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17
Q

Is threonine an essential amino acid?

A

Yes

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18
Q

Is tryptophan an essential amino acid?

A

Yes

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19
Q

Is valine an essential amino acid?

A

Yes

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20
Q

Is alanine an essential amino acid?

A

No

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21
Q

Is asparagine an essential amino acid?

A

No

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22
Q

Is aspartic acid an essential amino acid?

A

No

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23
Q

Is cysteine an essential amino acid?

A

No

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24
Q

Is glutamic acid an essential amino acid?

A

No

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25
Q

Is glutamine an essential amino acid?

A

No

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26
Q

Is glycine an essential amino acid?

A

No

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27
Q

Is proline an essential amino acid?

A

No

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28
Q

Is serine an essential amino acid?

A

No

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29
Q

Is tyrosine an essential amino acid?

A

No

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30
Q

Which amino acid should be avoided by diabetics as a supplement

A

Cysteine (interacts with insulin)

31
Q

Which amino acid is a precursor for serotonin?

A

Tryptophan

32
Q

Rigidity In the primary structure of polypeptides

A

Caused by carbon-nitrogen bond having partial double bond character.

33
Q

Interactions in the secondary structure of amino acids

A

Hydrogen bonds:
Beta pleated sheets
Alpha helix

34
Q

Which amino acid is a helix breaker

A

Proline

35
Q

Interactions within the tertiary structure

A 
Disulphide bridges (2 cysteine)
Hydrogen bonding
Electrostatic/ionic
Hydrophobic
Polar (OH)
36
Q

What is the quaternary structure

A

Multiple chains interacting forming subunits

37
Q

Types of super secondary structures

A

BaB unit

Greek key of B-pleats

38
Q

What is denaturation

A

Loss of proteins structure and thus function

39
Q

Causes of denaturation

A

Changes in pH
Salt conc
Temp
Environmental changes

40
Q

What aids protein folding

A

Chaperonins

41
Q

Ways to determine protein structure

A

X-Ray crystallography

NMR spectroscopy

42
Q

Result of protein misfolding

A

Loss or modification of activity

Aggregation

43
Q

Cause of sickle cell disease

A

Amino acid substitution in harmoglobin causes aggregation and fibres. Deformed RBCs

44
Q

Cause of Cystic fibrosis

A

Deletion of Phe in CFTR protein which is degraded.

45
Q

What is p53

A

Tumour suppression gene. Mutations present in tumour cells

46
Q

Cause of Alzheimers

A

B-amyloid cleaved from APP produces aggregations of plaques in the brain

47
Q

What is PrPc

A

Native form of prion protein mainly a-helix.

48
Q

What is PrPSc

A

Amyloidogenic form. Mix of B-sheets and a-helices. Aggregates form insoluble plaques in brain

49
Q

What causes huntingdons?

A

Huntingtin protein is longer than normal and end is cleaved to form aggregates and inclusions.

50
Q

What causes Parkinson’s?

A

Inclusions in the cytoplasm called Lewy bodies formed from multiple proteins.

51
Q

Cause of cataracts

A

Aggregation of crystallins due to environmental factors (UV or oxidising agents)

52
Q

Fibrous proteins

A

Filamentous elongated held by strong bonding

53
Q

Globular proteins

A

Compact structures that interact with other molecules e.g enzymes, antibodies

54
Q

Membrane proteins

A

Embed in membranes and transmit molecules in and out cell

55
Q

Structure of collagen

A

Triple helix. Repeating triplet of glycine, X (often proline) and Y (often hydroxyproline)

56
Q

Structure of glycerophospholipid

A

Two hydrophobic fatty acid tails joined to hydrophilic head (glycerol, phosphate and choline)

57
Q

Define steroid

A

Lipids with a carbon skeleton consisting of four fused rings

58
Q

Define ligand

A

Extra cellular signalling molecules

59
Q

Define a catalyst

A

Increases the rate of a chemical reaction without being changed itself. Cannot alter the position of equilibrium but allows equilibrium to be reached quicker.

60
Q

Define free energy of activation

A

Equal to the difference in free energy between the transition state and the substrate.

61
Q

Define induced fit of an enzyme

A

Frequent binding of substrate induces a conformational change in the active site.

62
Q

Factors affecting enzyme activity

A 
Substrate concentration
Enzyme concentration
Temperature
Post translational modification (e.g phosphorylation, Proteolytic activation)
Coenzymes and cofactors
pH
63
Q

Most coenzymes are related to what structural group

A

Vitamin B group

64
Q

What is end product feedback

A

Inhibits the committed step (first step to produce an intermediate unique to the pathway) earlier in the pathway.

65
Q

What is allosteric regulation

A

Molecules that regulate an enzymes activity by binding to a site remote from the active site.

66
Q

Define cooperativity

A

Binding of a substrate can trigger the same conformational change in all other subunits of the enzyme

67
Q

Define isoenzyme

A

Different forms of an enzyme which catalyse the same reaction

68
Q

What does LDH stand for

A

Lactate dehydrogenase

69
Q

Structure of LDH

A

2 subunits H and M. 5 different combinations

70
Q

Where is H4 and H3M found?

A

Mainly heart and RBCs

71
Q

Where is H2M2 LDH found?

A

Brain and kidney

72
Q

Where is HM3 and M4 LDH found?

A

Skeletal muscle and liver

73
Q

What does LDH isoenzymes in the blood indicative of?

A

Cell death. E.g myocardial infarction, infectious hepatitis and muscle diseases.

74
Q

What is a multi-enzyme complex

A

Aggregation of several enzymes/coenzymes into a single functional unit. Usually perform a multi-step transformation

Veterinary Medicine (3 decks)

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