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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 to increase the uptake of glucose by liver and muscle

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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 4 S-S Bridges, with 2 between 2 chains and 2 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 and Beta Sheet

A

HYdrogen bond between O and H atom

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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

What is the number of strand involved in each turn of Alpha helix

What is the size in Angstrong

A

3.6 amino acids

5.4Å (angstrom) per 360º turn

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13
Q

How many strands are involved in a Beta sheet

A

At least 2

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14
Q

Name the direction of the chains

A

Parallel or anti-parallel are ok

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15
Q

How do we described the zig-zag like appearance of Beta Sheet

A

Pleated

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16
Q

What contributes to a Tertiary structure

Name the 3 forces

A

Interactions between side chains

Hydrogen bond, VDW, electrostatic attraction

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17
Q

What contributes to a Quaternary Structure

A

Interactions between subunits

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18
Q

What is fibrous protein

What is their solubility in water

A

It has long, repetitive structures that enable structural role

And it is insoluble in water

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19
Q

What are the subunits of collagen. What is their orientation

A

3 left-handed Alpha-Helix

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20
Q

What is the orientation of collagen

A

A right-handed Super Helix

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21
Q

What is the recur in Collagen

A

Glycine-proline-hydroxyproline

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22
Q

When is hydroxyproline formed

A

Post-translational modification

23
Q

Name the higher lvl structure that collagen joins to form

24
Q

Describe and explain the appearance of fibrils

A

Striated as there are regular spaces between collagens

25
What is the chemical formula of Vitamin C
Sodium ascorbate
26
Why is Vitamin C required for the synthesis of collagen
To keep the Fe2+ ion reduced so that it can be the cofactor of prolyl 4-hydroxylase
27
What is the enzyme prolyl 4-hydrogenase for
Converting Proline to hydroxylproline
28
What is the component of Keratin and their orientation in the molecule
2 Alpha Helices to form a coiled coil structure
29
Name the higher level structures Keratin form
Protofilament--> Protofilbrils -->Intermediate filament
30
Name the force stabilizing the Keratin
S-S bridges between Cysteine amino acids
31
Does a RA/OA breaks the S-S bridges
RA
32
How to enhance the tensile strength of Keratin Can microbes feed on Keratin. What are they
Increase the number of S-S bridges Yes. Some infectious fungi
33
What is the solubilty of Globular Protein
Soluble in water
34
Name 2 oxygen-binding protein
Myoglobin and haemoglobin
35
Is the haem structure planar/3D Briefly describe the structure
Planar - Consists of a porphyrin ring and crown like structure with nitrogen - Nitrogens interact with central Fe2+ of haemoglobin/myoglobin - Histidine in backbone of myoglobin (and haemoglobin) - Distal histidine stabilises oxygen at that position - Oxygen ligand interacts with the distal E7 histidine
36
Is the myoglobin similar to the alpha/beta subunit of Hb
Beta
37
Where is the Myoglobin functioning
Muscles
38
How the Haemoglobin illustrates positive cooperativity
As it binds to more oxygen, the binding force becomes stronger and stronger
39
How can Hb exhibit the postitive cooperativity
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
40
What is the effect of Carbon monoxide binding on the haemoglobin
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
41
Name 2 differences between myoglobin and haemoglobin
Myoglobin has 1 subunit with 1 haem with Haemoglobin has 4 subunit and 4 haem
42
What are the proteins helping protein folding called. What is it's size, Does it use energy? Name 1 example
Chaperstone(GroEL) - Large protein complexes - Often uses energy (ATP) - Help fold proteins from its unfolded states GroEL
43
Can a protein be stable at 2 states? For lymphotacin, name the 2 forms Do the 2 term co-exist
Yes Chemokine form and Glycoaminoglycan-binding structure Yes. In equilibrium
44
Name 1 type of improperly folding protein that can cause disease and infectious
Prion diseases. Like Bovine Spongyform encephalopathy, Kuru, Scrapie and CJD
45
In Bovine Spongyform Encephalopathy, what is the difference in structure of normal protein (PrPC) and abnormal
PrPc has Fully Helix structure PrPsc has some beta sheets
46
Why mad cow disaese is infectious
The PrPSc can act as site of nucleation to convert more PrPc to PrPSC
47
What is the problem with Madcow disease improperly folded protein
It creates large fibres which aggregrate to form amyloid fibres in the brain
48
How is Alzemeir disease caused
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. The amyloid protein itself is normal but the acculmulation is toxic to the brain
49
Name 4 prion-related disease
CJD (Creutzfeldt-Jakob Disease) Kuru Bovine spongiform encephalopathy(BSE), aka Mad cow disease Scrapie
50
What is the Lock-and-Key Model about
The amino acid resifdue of the binding site are arranged in a complementary 3D surface that recognize the Subtrate The subtrate is bound via VDW, hydrogen bond and Electrostatic interaction
51
What is the Induced-Fit Model About
Induced-fit model - The substrate binding site is not a rigid pocket - It is a dynamic surface with flexible 3D structure - As the substrate binds, the side chains of the amino acids in the active site will reposition to interact with the substrate for the reaction to occur - E.g. glucose binding of hexokinase: - With the binding of glucose, the active site cleft of hexokinase closes - It is one of the largest induced fits known
52
What is THE MICHAELIS-MENTEN EQUATION
Vi= Initial Velocity V max= maximal velocity reached when infinite amount of subtrate was present Km (Michaelis Constant) is the concentration required to reach V max High Km = low affinity [S]= concentration of subtrate Vi = V max [S]/ (Km +[S])
53
What is the Enzymatic reactions concerning 2 subtrates What are the 2 types of the aforementioned reaction
BISUBSTRATE ENZYMATIC REACTIONS Sequential reactions (single displacement reaction): - Ordered: one substrate must bind first, before the second substrate can bind and a reaction can occur - Random order: no requirement of which substrate has to bind first for reaction to occur
54

MBBS IASM (24 decks)

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