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Bio /chem/cell > Proteins And Enzymes W2 > Flashcards

Proteins And Enzymes W2 Flashcards

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1
Q

Protein functions (8)

A 
Structure support 
Movement 
Transport 
Fluid balance 
acid base balance 
Energy production/glucose 
Immune function 
Enzymes hormones and neurotransmitters
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2
Q

In terms of structure and movement what role do proteins play (3)

A

Proteins required for
Synthesis
Maintenance
And repair

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3
Q

Main proteins involved in structure and movement

4

A

Collagen
Elastin
Keratin
Actin /myosin

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4
Q

Where is collagen found (6)

A 
Connective tissue 
Bone 
Cartilage
Ligaments 
Tendons 
Skin
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5
Q

Where is elastin found (6)

A 
Connective tissue 
blood vessels 
Lungs 
Ligaments 
Skin
Bladder cartilage
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6
Q

Where is keratin found (3)

A

Hair
Nails
Skin

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7
Q

Where is actin and myosin found (1)

A

Contractile proteins in muscle cell

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8
Q

Main proteins that act as
Catalysts (1)
Messengers (2)
And promote immunity (1)

A

Enzymes

Hormones
Neurotransmitters

Antibodies

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9
Q

Proteins - chem messengers - hormones

Example

A

Insulin increases glucose uptake

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10
Q

Proteins- catalysts- enzymes example

A

Pepsin breaks down polypeptides

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11
Q

Proteins- chem messengers - neurotransmitters example

A

Glycine is an inhibitory neurotransmitter in the CNS

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12
Q

Example of transport proteins in the blood: OXYGEN transported by…

A

Haemoglobin

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13
Q

Example of transport proteins in the blood: MINERALS (iron) transported by…

A

Transferrin protein

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14
Q

Example of transport proteins in the blood: FAT SOLUBLE VITAMINS transported by…

A

Retinal-binding protein

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15
Q

Example of transport proteins in the blood: HYDROPHOBIC LIPIDS is transported by…

A

Albumin

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16
Q

What is the most abundant plasma protein and what does it contribute to

A

Serum albumin

Oncotic pressure of plasma

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17
Q

Fluid balance: example of protein involvement

A

Hydrostatic pressure forces fluid out of capillaries and into
Interstitial space
Proteins remain in capillary and draw fluid back in –> maintaining fluid balance

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18
Q

Pretoria deficiency –> fewer blood proteins (serum albumin) —> ………?

A

Oedema

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19
Q

What property allows proteins to maintain acid base balance

A

Amino acids are amphoteric

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20
Q

Amphoteric meaning

A

Having both positive and negative regions of charge

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21
Q

Amino acids are amphoteric

What does this mean in terms of a proteins role in maintaining acid base balance

A

Protein can behave as both acid and base

Therefore can act as buffers and minimise changes in pH in blood

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22
Q

Which part of amino acid acts as an acid

A

Carboxyl group (releases a proton)

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23
Q

Which part of amino acid acts as a base

A

Amine group (binds a proton)

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24
Q

That is the body’s primary energy source (2) and where is it stored

A

Carbohydrates (muscle and liver)

Fat (adipose tissue)

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25
Q

How many calories of energy does 1 g of AA provide

A

4 cal

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26
Q

Do AA/proteins have specialised storage form ?

A

No

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27
Q

When AA/ proteins are required for energy production (eg during times of starvation) where are they taken from

A

Blood and body tissues

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28
Q

What happens when we consume excess protein

A

Deamination

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29
Q

During deamination where does the amine end go ?

A

Urea–> urine

30
Q

Where does the Leto acid go after deamination

A

Glucose
Fat
Energy

31
Q

What is the carboxyl/c-R section that is split during deamination called

A

Keto acid

32
Q

Protein turnover rate

A

200g/day

33
Q

What are three reasons that proteins may be degraded

A

Part of regular maintenance

Times of protein/energy deficiency

Tissue repair

34
Q

How can new proteins be synthesised(1)

2

A

From the bodies AA pool

  • those from diet
  • third released during protein breakdown
35
Q

Recommended dietary intake of protein

A

0.8g/kg of body weight

36
Q

We are in equilibrium when protein (N) intake =

A

nitrogen excretion

37
Q

Positive protein/nitrogen balance

A

(N) consumption > nitrogen excretion

38
Q

Negative protein/nitrogen balance

A

(N) consumption < nitrogen excretion

39
Q

Upper limit of protein intake

A

25% if KJ consumed

40
Q

What happens when you eat too much protein (risks) (3)

A

Increase risk of health problems and disease

Increase urea + Uric acid due to increase in deamination

Loss of essential minerals

41
Q

Risks of too much protein–> increased urea and Utica acid due to increased deamination

–> complications (2)

A

Increased water loss (dehydration)

Gout (Uric acid build up in joints)

42
Q

What is gout

A

Utica Acid build up in joints

43
Q

Protein deficiency risks (5)

A

Anaemia

Impaired growth

Muscle wasting

Weakened immune system

Oedema

44
Q

What are enzymes

A

Globular proteins

45
Q

Enzymes have crucial roles in : (4)

A

Digestion of food

Energy production

Making proteins and body structures

Storing nutrients

46
Q

Enzymes are not ….. or …… in a reaction

A

Consumed

Changed

47
Q

What do enzymes bind to

A

One or more reactants/substrates

48
Q

Enzymes convert ….. to ……

A

Substrate

Product

49
Q

Enzymes are very specific

How?

A

They have complementary shape to the substrate

And this sharpe is offering of every substrate

50
Q

How do enzymes bind to substrates
To what
What bonds

A

Cluster of AA side chains
Forming non covalent bonds
(H bond , hydrophobic interactions)

51
Q

What affects enzyme reactions (2)

A

Temperature

pH

52
Q

How does temperature affect enzyme reactions

A

Increases rate of reaction but causes enzymes to denature

53
Q

Temperatures over …. C are destructive to enzymes

A

50 C

54
Q

What is tolerated better HYPERthermia or HYPOthermia

A

HYPOthermia (cold temperatures)

55
Q

How does pH affect enzyme activity

A

Influences state of ionisable groups on the protein

56
Q

Metabolic pathways can be controlled by regulating …….

A

Enzyme activity

57
Q

How are enzymes regulated (6)

A
  • self regulated
  • enzyme inhibition
  • gene induction and repression(increase and decrease of enzyme production)
  • phosphorylation
  • allosterism
  • proteolytic activation
58
Q

2 types of enzyme inhibition

A

Competitive/noncompeditive

59
Q

2 types of competitive/non competitive inhibition

A

Reversible/irreversible

60
Q

What do competitive inhibitors do

A

Interferes with active site of enzyme so substrate cannot bind

61
Q

What do non competitive inhibitors do

A

Bind to no active site of enzyme and change shape of enzyme so it can’t bind to substrate

62
Q

What is proteolytic activation

A

Activating and enzyme by peptide cleavage

63
Q

Proteolytic activation is common with ……. …….

A

Digestive enzymes

64
Q

Example of enzyme that is activated via proteolytic activation

A

Protein digesting enzyme

Trypsin

65
Q

Pathway of trypsin and proteolytic activation

A

Trypsinogen released from pancreas into small intestine in inactive form

Enzymes in small intestine cleave the molecule and activate it –> trypsin

Trypsin may begin its role in digestion

66
Q

What is the inactive for of trypsin called

A

Trypsinogen

67
Q

Where is trypsinogen released from and where is it released into

A

Released From Pancreas

To small intestine

68
Q

Some enzymes are purely protein, other have two parts ….. and …….

A

Apoenzyme (protein part)

Co factor

69
Q

Co factors may be an ……. or an ……..

A 
Ion 
Organic molecule (vitamin)
70
Q

Examples of co factors (3)

A

Manganese
Magnesium
Calcium

Bio /chem/cell (13 decks)

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