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MBBS IASM > Protein > Flashcards

Protein Flashcards

1
Q

How does Insulin work

A

It causes confrontmation change in the insulin receptor and bring more glucose transporter to the cell membrane to facillate Glucose Uptake

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2
Q

What is the next step for glucose

A

Converted into Glycogen at the place where glycogenesis takes place

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3
Q

Describe the structure of insulin

A

By 2 polypeptide chain, by 3 S-S Bridges, with 2 between 2 chains and 1 within the peptide

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4
Q

What is the backbone of a chain formed by 3 amino acids

A

NCaCNCaCNCaC

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5
Q

What is the number of amino acids in a (i)protein (ii)peptide

A

(i)>100 (ii)<100

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6
Q

Leu-Cys-Pro shows what order of protein structure

A

Primary

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7
Q

What is a secondary structure

A

Local confrontmation of the backbone due to the interactions between atoms at the backbone

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8
Q

Name 2 commonly seen Secondary Structure

A

Alpha Helix, Beta Sheet

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9
Q

(i) What are the bonds stabilizing Alpha Helix

A

HYdrogen bond

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10
Q

(ii) Are the side chains pointing inwards or outwards in Alpha Helix

A

Outwards

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11
Q

(iii) What is the orientation of most Alpha Helices

A

Right-handed

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12
Q

How many strands are involved in a Beta sheet

A

At least 2

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13
Q

Name the direction of the chains

A

Parallel or anti-parallel are ok

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14
Q

What contributes to a Tertiary structure

A

Interactions between side chains

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15
Q

What is fibrous protein

A

It has long, repetitive structures that enable structural role

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15
Q

What contributes to a Quaternary Structure

A

Interactions between subunits

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16
Q

Is fibrous protein soluble in water?

A

No

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17
Q

What are the subunits of collagen. What is their orientation

A

3 left-handed Alpha-Helix

18
Q

What is the orientation of collagen

A

A right-handed Super Helix

19
Q

Name the 3 amino acids Collagen is rich in

A

Proline, Hydroxylproline, Glycine

20
Q

Name the higher lvl structure that collagen joins to form

A

Fibrils

21
Q

Describe and explain the appearance of fibrils

A

Striated as there are regular spaces between collagens

22
Q

What is the chemical formula of Vitamin C

A

Sodium ascorbate

23
Q

Why is Vitamin C required for the synthesis of collagen

A

To keep the Fe2+ ion reduced so that it can be the cofactor of prolyl 4-hydroxylase

24
Q

What is the enzyme prolyl 4-hydrogenase for

A

Converting Proline to hydroxylproline

25
Q

What is the component of Keratin and their orientation in the molecule

A

2 Alpha Helices to form a coiled coil structure

26
Q

Name the higher level structures Keratin form

A

Protofilament–> Protofilbrils –>Intermediate filament

27
Q

Name the force stabilizing the Keratin

A

S-S bridges between Cysteine amino acids

28
Q

Does a RA/OA breaks the S-S bridges

A

RA

29
Q

What is the solubilty of Globular Protein

A

Soluble in water

30
Q

Name 2 oxygen-binding protein

A

Myoglobin and haemoglobin

31
Q

Is the haem structure planar/3D

A

Planar

32
Q

Is the myoglobin similar to the alpha/beta subunit of Hb

A

Beta

33
Q

Where is the Myoglobin functioning

A

Muscles

34
Q

How the Haemoglobin illustrates positive cooperativity

A

As it binds to more oxygen, the binding force becomes stronger and stronger

35
Q

How can Hb exhibit the postitive cooperativity

A

Binding of oxygen to haem increases oxygen affinity by inducing structural changes
in the adjacent globin chains, turning the haemoglobin from a Tense state to a Relaed
shape. This positive cooperativity within haemoglobin is responsible for a
sigmoidal-shaped oxygen dissociation curve

36
Q

What is the effect of Carbon monoxide binding on the haemoglobin

A

The binding of one CO molecule to haemoglobin increases the affinity of the other
binding spots for oxygen, leading to a left shift in the dissociation curve. This shift
prevents oxygen unloading in peripheral tissue and therefore the oxygen
concentration of the tissue is much lower than normal

37
Q

Name 2 differences between myoglobin and haemoglobin

A

Myoglobin has 1 subunit with 1 haem with Haemoglobin has 4 subunit and 4 haem

38
Q

What are the proteins helping protein folding called. Name 1 example

A

Chaperstone(GroEL)

39
Q

Name 1 type of improperly folding protein that can cause disease and infectious

A

Prion diseases. Like Bovine Spongyform encephalopathy, Kuru, Scrapie and CJD

40
Q

In Bovine Spongyform Encephalopathy, what is the difference in structure of normal protein (PrPC) and abnormal

A

PrPc has Fully Helix structure
PrPsc has some beta sheets

41
Q

Why mad cow disaese is infectious

A

The PrPSc can act as site of nucleation to convert more PrPc to PrPSC

42
Q

What is the problem with Madcow disease improperly folded protein

A

It creates large fibres which aggregrate to form amyloid fibres in the brain

43
Q

How is Alzemeir disease caused

A

The Amyloid-Beta peptide self-associates into fibrils then into amyloid plaque.

The improper form has more Beta sheets than the original amyloid precursor protein(APP), leading to aggregation.

MBBS IASM (13 decks)

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