proteins part 2 Flashcards

1
Q

What are the different types of proteins?

A

structural e.g. keratin
enzymatic e.g. digestive enzymes
contractile e.g. myosin
receptor e.g. g proteins
defensive e.g. immunoglobulins
hormonal e.g. insulin
storage
transport e.g. haemoglobin

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2
Q

What is post translational modification?

A

subsequent modification after protein been transcribed

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3
Q

What is co translational modification?

A

modification at same time as translation

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4
Q

What are the three types of conjugated proteins?

A

glycoproteins
lipoproteins
metalloproteins

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5
Q

What are glycoproteins?

A

Proteins with ≥1 carbohydrate molecule(s) covalently attached

Co-translational or post-translational
modification where oligosaccharide chains are attached to a protein

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6
Q

Effects of glycosylation?

A

1.Stability
2.Solubility
3.Cell signalling
4.Orientation

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7
Q

How is blood transfusion compatibility achieved?

A

The immune system recognizes the combo of carbs present upon or absent from the surface of an erythrocyte

if deemed by immune system to be foreign, immune system secretes particular antibodies to effectively clump the foreign red blood cells together

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8
Q

Why can we use glycoproteins for diagnostic purposes?

A

patients with undiagnosed diabetes mellitus have high levels of glucose in blood

excess glucose binds to haemoglobin within erythrocytes forming glyco proteins

can detect the concentration of these glycoproteins in a patient’s blood

and since erythrocytes only stay in circulation for 100 days , conc will correlate with patients blood sugar levels occurring over that period of time

therefore patients with diabetes or suspected allow clinicians to obtain a useful snapshot of average blood glucose control

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9
Q

HbA1C?

A

pathological glycoprotein

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10
Q

What are lipoproteins?

A

proteins combined with lipids

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11
Q

Where are lipoproteins found?

A

In cell membranes and transporting hydrophobic molecules around aqueous bloodstream

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12
Q

What are apolipoproteins?

A

lipoproteins with other lipoproteins

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13
Q

What do apolipoproteins do?

A

transport fat, fat soluble vitamins and fat soluble hormones around the body within blood and cerebral spine fluid

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14
Q

What are metalloproteins?

A

Protein molecules with a metal ions within
their structures (co-factors)
Various functions (e.g. enzymatic, signal
transduction, storage and transport

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15
Q

Describe structure of haemoglobin?

A

large quaternary structure, four polypeptide chains , two alpha subunits and two beta subunits.
The interfaces where subunits meet are usually non polar and this plays important role in transmitting information
Each subunit contains an organic molecule called heme and inside heme molecule sits an atom of iron

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16
Q

What allows haemoglobin to transport one mol of oxygen?

A

Interaction between iron, heme and polypeptide subunit. Each haemoglobin mol with four subunits can carry four mols of oxygen

17
Q

What does the amount of oxygen that can be dissolved in blood depend on?

A

partial pressure of oxygen within lung alveoli.

18
Q

How much oxygen does plasma in working normally lungs have?

A

plasma leaving lungs has almost as much dissolved oxygen as is possible
plasma can only carry a max of 3ml oxygen per l

19
Q

What are the effects of sickle cell blood disease?

A

sickle cells struggle to pass through capillaries and inefficient in delivery oxygen to end tissues

20
Q

How does sickle cell disease arise?

A

GAG in normal beta chain changes to GTG, changes tertiary and quaternary.
Polar glutamine becomes non polar valine

21
Q

What are the the types of protein based on structure?

A

globular
fibrous
membranous

22
Q

What are the functions of globular Proteins?

A

storage
enzymes
hormones
transporters
structural

23
Q
A
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Q
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24
Q
A