Week 5 Proteins and Disease Flashcards

1
Q

What are all the different type of proteins?

A

Structural proteins, storage proteins, transport proteins, hormonal proteins, motor proteins, receptor proteins, defensive proteins and enzymatic proteins

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2
Q

What is an example of a structural proteins?

A

Keratin found in hair, feather, insects silk

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3
Q

What’s an example of storage proteins?

A

Protein of milk for baby animals (amino acids storage)

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4
Q

What’s an example of transport protein?

A

Transport of substances such as haemoglobin (iron protein)

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5
Q

What’s an example of hormonal protein?

A

Insulin, a hormone which regulates blood sugars

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6
Q

What’s an example of Motor proteins?

A

The movement of the cilia and flagella which causes contraction

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7
Q

What’s an example of receptor proteins?

A

Chemical stimulation sensing such as receptors in membranes

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8
Q

What’s an example of defensive proteins?

A

Protection against disease like antibodies de-ativiating a virus and bacteria

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9
Q

What’s an example of enzymatic proteins?

A

Selective acceleration of chemical reactions

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10
Q

What are the building blocks of proteins?

A

Amino acids joined in peptide bonds (20)

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11
Q

What does it mean if amino acids are hydrophilic or hydrophobic (state change on amino acids)

A

Hydrophobic are non-polar, whereas hydrophilic are polar and can be polar charged or polar un-charged

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12
Q

What is really meant by primary structure of protein?

A

Sequence of amino acids

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13
Q

How can you tell the difference between primary structure protein and secondary structure protein?

A

Secondary structure has short folded protein chain of weak hydrogen bonds

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14
Q

Picture a primary and secondary protein structure?

A

Primary is the long snake like, purple circle amino acids, whereas the secondary structure is the short folded single-stranded-helix-looking thing with weak hydrogen bonds

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15
Q

What is meant by a proteins quaternary structure?

A

protein chains/ sub-units packed closely together

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16
Q

What are quaternary structures held together by?

A

Stabilised by weak hydrogen bonds likeq

17
Q

Picture a quaternary protein structure?

A

Ball with haemoglobin and subunits a and b (at both sides) (see page 20 on week 5)

18
Q

What causes protein to unravel?

A

pH, salt concentrations, temperatures and environmental differences

19
Q

What terms describes when a protein loses its structure?

A

denatured protein

20
Q

What is the difference between denatured protein and protein?

A

denatured protein is in-active

21
Q

Picture normal protein and denatured protein?

A

Normal protein is like long string together, denatured is like long string far apart (see page 24)

22
Q

What process is it which a denatured protein can become normal protein again?

A

renaturation

23
Q

What are chaperonins?

A

Protein molecules which assist with the folding of other proteins

24
Q

What’s an example of a disease where chaperonins are defective?

A

Alzheimers and parkinsons and mad cow disease

25
Q

What can cause protein misfolding?

A

Mutations in gene encoding proteins, lack of enzyme in chaperons for protein folding, interaction with other misfiled proteins

26
Q

What could two protein related diseases be due to?

A

In sufficient amount of proteins for proper function (cystic fibrosis) and non-functional proteins

27
Q

What is sickle cell disease?

A

It is caused by a single substitution in the amino acids in protein haemoglobin