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Bio /chem/cell > AA and proteins -W1 > Flashcards

AA and proteins -W1 Flashcards

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1
Q

What elements make up carbohydrates

A

C H O

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2
Q

What elements make up lipids

A

C H O

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3
Q

What elements make up proteins

A

C H O N

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4
Q

Primary macronutrients

A

Carbs
Protein
Fats
Water

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5
Q

What are macronutrients and primary functions

A

Needed in larger amounts to support normal function

Provide energy 
Growth
Maintenance 
Support/structure 
Regulate body processes
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6
Q

Primary micronutrients

A

Vitamins

Minerals

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7
Q

What are micronutrients and primary function

A 
Required in smaller amounts 
key roles in metabolism 
Structure 
Growth 
Maintenance 
Regulation
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8
Q

How many types of amino acids are there

A

20

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9
Q

Structure of amino acid

A 
Amino end (NH2)
Carboxyl end (C=O, OH)
R group
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10
Q

What does the property of an amino acid depend on

A

R side chain

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11
Q

Properties of R side chain on AA and subsequent location

A

Charged, polar, hydrophilic - usually exposed on surface

Non polar
Hydrophobic - buried in hydrophobic interior or fire of proteins

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12
Q

AA used for…

A

Building proteins
Energy production
Converted to glucose
Precursors for: hormones, neurotransmitters, melanin

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13
Q

In a protein AA are held together by what type of bond

How is this bond made

A

Peptide bond

Dehydration synthesis

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14
Q

What determines the primary structure if a protein

A

DNA

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15
Q

What determines secondary and tertiary protein structures and functions

A

Primary structure

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16
Q

What bonds form secondary protein structures

Between what

A

H bonds
Between
H of amino group
O of carboxyl group

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17
Q

What are the two types of secondary protein structures

A

Alpha helices

Beta pleated sheets

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18
Q

In alpha helices

The backbone is more stable in a ………… helix

A

Right handed (clockwise)

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19
Q

What bonds are formed in formation of tertiary structures

Between what

A 
Hydrogen 
Ionic 
Van der walls forces 
Hydrophobic interactions 
Disguise bonds

Between AA R-group side chains

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20
Q

What bonds are present in quaternary structures

A

Weak interactions

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21
Q

Two types of protein classification

A

Globular

Structural

22
Q 
Structural proteins (fibrous) 
characteristics 
Use
A

Insoluble
Low turnover

Ideal for mechanical support and strength

23
Q 
Globular proteins (functional)
characteristics
A 
Compact 
Spherical 
Soluble 
Chemically active 
High turnover
24
Q

Structural proteins example

A

Collagen
Keratin
Elastin

25
Q

Globular proteins example

A

Enzymes
Hormones
Antibodies
Receptors

26
Q

Where is haemoglobin found

A

RBC

27
Q

Haemoglobin main function

A

Oxygen transport

28
Q

Haemoglobin composition

A

4 polypeptide chains (globin)

4 non-protein haem groups

29
Q

What can happen if haemoglobin if folded incorrectly

A

Sickle cell anaemia

30
Q

Collagen makes up …….% of protein in the body

A

25%

31
Q

How is collagen dispersed until he body

A

As gel

Or tightly bundled

32
Q

Collagen: what could go wrong

A

Osteogenesis imperfecta
(Brittle bone disease)

Scurvy

33
Q

Osteogenesis imperfecta

Brittle bone disease

A

Collagen formation- Glycine replaced by by other AA with bulky side chain
Prevents formation of triple helix structure
Bones easily fracture
Poor wound healing

34
Q

Scurvy

A

Collagen formation
Caused by lack of Vitamin C (involved in forming cross links between triple helices -making collagen fibril)
Decreases tensile strength
Causes brushing teeth fallout bleeding gums

35
Q

‘Denatured’ protein , ie……

A

Disruption of interactions/bonds of secondary, tertiary, quartenary structures

  • -> unfolding
  • -> loss of function
36
Q

What causes denatured proteins

A

pH
Temperature
Solvents
Chemical modification

37
Q

Denatured proteins- pH

A

Acids and bases disrupt ionic charge between SIDE CHAINS

Eg
Protein digestion in stomach

38
Q

Denatured proteins- temperature

A

Heat –> energy –> breaking bonds
Causing unfolding

Eg
Sterilising medical instruments with heat to denatured proteins in bacteria

39
Q

Denatured proteins- solvents

A

Disrupts SIDE CHAIN bonding
Eg
Alcohol disinfectant
Penetrates bacteria cell wall and denatured proteins and enzymes

40
Q

Denatured proteins- chemical modification

A

Eg
Oxidation
Glycosylation

41
Q

1g protein = ?? Cal

A

4.2

42
Q

Conversion factor from cal –> kj

A

~ x4

43
Q

Protein

Recommended dietary intake

A

0.8g/kg of body weight

44
Q

Protein is …….% of total energy intake

A

15-25

45
Q

Dietary protein- animal products

A

Meat
Dairy
Eggs

46
Q

Dietary protein- plant products

A

Soy
Legumes
Whole grains
Nuts

47
Q

How many essential AA

A

9

48
Q

A deficiency in just 1 AA can result in

A

Decreased protein synthesis

49
Q

Benefits / negatives of animals as a source of protein

A

Have similar AA profile to humans

higher levels of sat fats
lower in fibre
Less micronurients

50
Q

Benefits and negatives (exception) of plants as a source of protein

A

More fibre and micronutrients

Need to eat more and a larger variety to get all amino acids - can have low levels of one or more AA (different chem profile)

Exception = soybeans

Bio /chem/cell (13 decks)

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