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Proteins And Enzymes W2 Flashcards

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
How many calories of energy does 1 g of AA provide
4 cal
26
Do AA/proteins have specialised storage form ?
No
27
When AA/ proteins are required for energy production (eg during times of starvation) where are they taken from
Blood and body tissues
28
What happens when we consume excess protein
Deamination
29
During deamination where does the amine end go ?
Urea--> urine
30
Where does the Leto acid go after deamination
Glucose Fat Energy
31
What is the carboxyl/c-R section that is split during deamination called
Keto acid
32
Protein turnover rate
200g/day
33
What are three reasons that proteins may be degraded
Part of regular maintenance Times of protein/energy deficiency Tissue repair
34
How can new proteins be synthesised(1) | 2
From the bodies AA pool - those from diet - third released during protein breakdown
35
Recommended dietary intake of protein
0.8g/kg of body weight
36
We are in equilibrium when protein (N) intake =
nitrogen excretion
37
Positive protein/nitrogen balance
(N) consumption > nitrogen excretion
38
Negative protein/nitrogen balance
(N) consumption < nitrogen excretion
39
Upper limit of protein intake
25% if KJ consumed
40
What happens when you eat too much protein (risks) (3)
Increase risk of health problems and disease Increase urea + Uric acid due to increase in deamination Loss of essential minerals
41
Risks of too much protein--> increased urea and Utica acid due to increased deamination --> complications (2)
Increased water loss (dehydration) Gout (Uric acid build up in joints)
42
What is gout
Utica Acid build up in joints
43
Protein deficiency risks (5)
Anaemia Impaired growth Muscle wasting Weakened immune system Oedema
44
What are enzymes
Globular proteins
45
Enzymes have crucial roles in : (4)
Digestion of food Energy production Making proteins and body structures Storing nutrients
46
Enzymes are not ..... or ...... in a reaction
Consumed | Changed
47
What do enzymes bind to
One or more reactants/substrates
48
Enzymes convert ..... to ......
Substrate | Product
49
Enzymes are very specific | How?
They have complementary shape to the substrate | And this sharpe is offering of every substrate
50
How do enzymes bind to substrates To what What bonds
Cluster of AA side chains Forming non covalent bonds (H bond , hydrophobic interactions)
51
What affects enzyme reactions (2)
Temperature | pH
52
How does temperature affect enzyme reactions
Increases rate of reaction but causes enzymes to denature
53
Temperatures over .... C are destructive to enzymes
50 C
54
What is tolerated better HYPERthermia or HYPOthermia
HYPOthermia (cold temperatures)
55
How does pH affect enzyme activity
Influences state of ionisable groups on the protein
56
Metabolic pathways can be controlled by regulating .......
Enzyme activity
57
How are enzymes regulated (6)
- self regulated - enzyme inhibition - gene induction and repression(increase and decrease of enzyme production) - phosphorylation - allosterism - proteolytic activation
58
2 types of enzyme inhibition
Competitive/noncompeditive
59
2 types of competitive/non competitive inhibition
Reversible/irreversible
60
What do competitive inhibitors do
Interferes with active site of enzyme so substrate cannot bind
61
What do non competitive inhibitors do
Bind to no active site of enzyme and change shape of enzyme so it can't bind to substrate
62
What is proteolytic activation
Activating and enzyme by peptide cleavage
63
Proteolytic activation is common with ....... .......
Digestive enzymes
64
Example of enzyme that is activated via proteolytic activation
Protein digesting enzyme | Trypsin
65
Pathway of trypsin and proteolytic activation
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
What is the inactive for of trypsin called
Trypsinogen
67
Where is trypsinogen released from and where is it released into
Released From Pancreas | To small intestine
68
Some enzymes are purely protein, other have two parts ..... and .......
Apoenzyme (protein part) | Co factor
69
Co factors may be an ....... or an ........
``` Ion Organic molecule (vitamin) ```
70
Examples of co factors (3)
Manganese Magnesium Calcium

Bio /chem/cell (13 decks)

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