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BAMS > General Biochemistry Flashcards > Flashcards

General Biochemistry Flashcards

1
Q

What are prokaryotic cells

A

They comprise bacteria, they are relatively simple and have no true nucleus and no internal membrane bound organelles

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2
Q

What are eukaryotic cells

A

Found in higher animals and plants
Large complex molecules

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3
Q

What is the function of the plasma membrane

A

Semi permeable barrier between cytoplasm and external enviroment

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4
Q

What is the function of the nucleus

A

Controls cell activity

DNA found here

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5
Q

What is the role of the nucleolus

A

Ribosomes constructed here

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6
Q

Where is the site of transcription

A

The nucleus

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7
Q

What is the role of ribosomes

A

Main role id to facilitate protein translation

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8
Q

What is the rough endoplasmic reticulum

A

Contains ribosomes
Protein modification and production

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9
Q

What is the smooth endoplasmic reticulum

A

Predominant function is manufacturing of lipids
No ribosomes

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10
Q

What role does the smooth ER play in the liver

A

Converts organic chemicals into safer water soluble products
In the liver can double the surface area

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11
Q

Function of the golgi aparatus

A
  • further modifies proteins
  • stores proteins
  • packages proteins
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12
Q

Function of vacuoles

A

Used as storage areas

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13
Q

Function of vesicles

A

Function in transport

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14
Q

Function of lysosomes

A

The breakdown of extracellular materials, large vesicles formed by the Golgi apparatus

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15
Q

Function of mitochondria

A

Powerhouse of the cell
ATP formation

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16
Q

What are the two membranes of the mitochondria

A
  • outer membrane - smooth and sieve like
  • inner membrane folded into CRISTAE - surfaces on which ATP is generated
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17
Q

Function of the cytoplasm

A

Facilitates transport of material around the cell

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18
Q

What is the cytoskeleton

A

In eukaryotic cells there are fibrous proteins in the cytoplasm known as the cytoskeleton
- maintain shape of cell
- anchors organelles

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19
Q

What is a buffer

A

A solution which resists change in pH when acid or alkali is added to it

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20
Q

What is the major buffer in saliva

A

Bicarbonate

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21
Q

How do you calculate the pH from the hydrogen ion concentration of a solution

A

pH = -log10(H+)

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22
Q

What is the pH of a solution with (H+) of 0.00001M

A

PH 5

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23
Q

What are acids

A

A substance which in water tends to produce H+ ions

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24
Q

What is a base

A

A substance which in water tends to combine with H+ ions

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25
Q

What is the relationship between the strength of acid and Ka value

A

The stronger the acid the higher the Ka and the lower the pKa

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26
Q

What is Ka

A

The acid dissociation constant

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27
Q

What is pKa

A

A number that describes the acidity of a particular molecule

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28
Q

What is the Henderson-Hasselbalch Equation

A

pH = pKa+log10(B-)/(A)

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29
Q

How do you calculate pKa

A

pKa=-log10Ka

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30
Q

What are buffer solutions made of

A

Consist of a conjugate acid base pair of either a weak acid or weak base

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31
Q

What is the role of buffering in the body

A

Maintains body pH homeostasis

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32
Q

Why is buffering in the mouth important

A

Limits pH changes due to acid production by plaque bacteria

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33
Q

When is buffering most effective

A

When concentration of acid = concentration of conjugate base

34
Q

When do buffers operate optimally

A

When half dissociated

35
Q

Important buffers in saliva

A

Histatins
Bicarbonate
Phosphate

36
Q

What acids are produced by oral bacteria

A
  • lactic acid
  • formic acid
  • acetic acid
  • propionic acid
  • butyric acid
37
Q

What is tooth erosion caused by

A

A direct result of acid in the diet on the teeth

38
Q

What are the 3 different pKa values that bicarbonate acts as a buffer

A

PKa = 2.16, 7.21, 12.32

39
Q

What are chelating agents

A

Chemical compounds that bound tightly to metal ions

Could have an erosive effect on teeth

Fruit juices contain chelating agents

40
Q

What are some biological roles of proteins

A
  • transport
  • storage
  • catalysts
  • motion
41
Q

What is electronegativity

A

The power of an atom to attract electrons towards itself

42
Q

Where are L isomers found

A

Proteins

43
Q

Where are D isomers found

A

Bacterial cell walls

44
Q

What is a primary structure of a protein

A

Amino acid sequence

45
Q

What is secondary structure of a protein

A

Regions of amino acid chains that are stabilised by hydrogen bonds between chains

46
Q

What is tertiary structure of a protein

A

3D arrangement of all atoms in polypeptide chains

47
Q

What is quaternary structure of a protein

A

3D interaction of protein subunits in proteins with more than one polypeptide

48
Q

What is an alpha helix

A

Secondary structure of protein
Rod like
Found in strong extensible proteins

49
Q

Describe B pleated sheet

A

Zigzag chains
Found in proteins where flexibility is needed

50
Q

What protein has the triple helix structure

A

Collagen only
Major component of connective tissue

51
Q

What are fibrous proteins

A

Insoluble, metabolically unreactive

Collagen, keratin, fibrin ect

52
Q

What are globular proteins

A

Spherical
Water soluble
Myoglobin and actin are examples

53
Q

What is the role of myoglobin

A

Oxygen storage in muscle

54
Q

What is haemoglobbin composed of

A

2 alpha and 2 beta chains

55
Q

Name some examples of messenger proteins

A

Insulin
Glucagon
Human growth hormone

Just hormones in general

56
Q

What are the monomers of polysaccharides

A

Monosaccharides

57
Q

What are the functions of polysaccharides

A

Storage and structure

Glycogen starch for example

58
Q

What are the monomers of lipids

A

Fatty acids

59
Q

What reactions of monosaccharides form disaccharides

A

Dehydration and hydrolysis

60
Q

What are sterols

A

Lipids with some essential biological activity

61
Q

What does caries involve

A

Acids that are produced by plaque bacteria

62
Q

How does fluoride act to reduce tooth solubility

A

1) reduces enamel solubility at low pH
2) inhibits bacterial metabolism of carbohydrates
3) promotes enamel remineralisation by saliva

63
Q

What inhibits solubilisation of enamel

A

An increase in calcium or phosphate concentration will shift the equilibrium to the left this inhibits solubilisation and inhibit remineralisation

64
Q

What is a null hypothesis

A

States there is no significant difference between two variables in a hypothesis

65
Q

What are enzymes

A

Enzymes are biological catalysts

66
Q

How do enzymes act

A

Accelerate the time it takes to reach equilibrium

67
Q

What is the role of amylase

A

Found in saliva, converts starch into sugars

68
Q

What is the role of maltose

A

Breaks the sugar maltose into glucose

69
Q

How do enzymes work

A

Lock and key model
Induced fit model

70
Q

What are enzymes usually

A

Proteins

71
Q

What is the standard free energy change

A

The difference between energies of reactants and products

72
Q

What does reaction rate depend on

A

Reaction rate depends on the activation energy

73
Q

What is the activation energy

A

The energy input required to initiate a reaction

74
Q

What is the effect of an enzyme on activation energy

A

Lowers activation energy

75
Q

What factors can affect the rate of an enzyme reaction

A
  • temperature
  • pH
  • enzyme/substrate concentration
  • inhibitors and activators
  • covalent modification
76
Q

What is V max

A

Maximum reaction rate

77
Q

What is Km

A

The substrate concentration at which half of the maximum velocity is achieved

78
Q

What is an irreversible inhibitor

A

Damages enzymes beyond repair
Generally cause covalent modifications of the enzyme

79
Q

What is a reversible inhibitor

A

Full enzyme activity is regained when the inhibitor is removed

80
Q

What is feedback inhibition

A

Control of metabolic pathways often occurs by feedback inhibition this is often done by the product of the pathway acting as an inhibitor on an earlier step in the pathway

81
Q

What is the different between a competitive and non competitive inhibitor

A

Competitive - substrate and inhibitor compete for the same binding site
Non competitive - bind to an allosteric site on the enzyme

82
Q

What are allosteric enzymes

A

Possesses multiple subunits

Contains a region in which small effector molecules can bind

Positive modulators - increase affinity for active site
Negative modulators - decrease affinity for activity site

BAMS (41 decks)

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