Class 1 Flashcards

(30 cards)

1
Q

What is the primary structure of a protein?

A

Sequence of AAs

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
2
Q

What is the secondary structure of a protein?

A

H bonding between back bone

-helix, beta sheet

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
3
Q

What is the tertiary structure of a protein ?

A

Side chain interactions with a polypeptide

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
4
Q

What is the quaternary structure of a protein?

A

Side chain interaction between different polymers/groups of proteins

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
5
Q

In the tertiary protein structure, what are the different kinds of non covalent bonds?

A

non polar - nonpolar
Polar-polar (uncharged)
Electrostatic (acid/base) charged

these brake with acid/base, heat and salt solution

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
6
Q

In the tertiary protein structure, what are the different kinds of covalent bonds?

A

disulphide bridges fir Cystein (cys) C

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
7
Q

How aree starch cellulose and glycogen all linked together?

A

alpha 1,4 (linear) and alpha 1,6 = starch and glycogen

beta 1,4 = cellulose

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
8
Q

What are carbs used for?

A

Energy
Cell surface markers
Adhesion

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
9
Q

What is a transfat?

A

Take. unsaturated fat and add hydrogens and force it to become solid
-reduces double bonds and some go to trans double bonds

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
10
Q

What are Triglycerides?

A

3 FA and a glycerol

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
11
Q

How are TGs made?

A

Dehydration synthesis

Forms ester bonds during synthesis

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
12
Q

What are terpenes?

A

Made from isoprene units (need at least 2)

They are waxes, precursors to this are ring lipids and Vitamin A

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
13
Q

What is the structure of steroids and cholesterol ?

A

3 cyclohexane and 1 cyclopentane

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
14
Q

What does G, H and T and S mean?

A

G free energy
H Enthalpy
T temp
S entropy

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
15
Q

What happens when G is positive of negative?

A

G>0 its non spontaneous (potential is greater than kinetics)

G<0 its spontaneous (potential is less than kinetics)

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
16
Q

What does exergonic mean?

A

spontaneous, so it will happen at some point, but doesn’t mean its fast

17
Q

Are transition states stable?

A

No they have increased. energy and are unstable and won’t last long

18
Q

Why are lower activation energies more stable?

A

Increases stabilization of transition state

Reduce activation energy

19
Q

Are enzymes. always on?

A

Yes, you need tp phosphorylate it to turn the enzyme on or off

20
Q

What is allosteric regulation?

A

Regulate enzymes via conformation change

21
Q

What is a negative feedback?

A

Product inhibits something at the start of the chain

22
Q

What its a positive feedback?

A

Drives the formation of the products (not for regulation) but must have external regulator to stop

23
Q

What does max depend on?

A

[Enzyme]

Type of enzyme you’re working with

24
Q

What is the Km?

A

Concentration of the substrate required to reach 1/2 Vmax

-the affinity it has for the substrate

25
What happens when substrate affinity increases?
Km decreases
26
What are the 4 kinds of inhibition?
Competition Non competition Uncompetitive Mixed inhibitors
27
What is competition inhibition?
Binds active site Vmax is unchanged Km: increases (low affinity)
28
What is the non competition inhibition?
Binds allosteric site of enzyme Vmax decreases Km unchanged
29
What is uncompetitive inhibition?
Binds allosteric site of enzyme substrate complex Vmax decreases Km decreases
30
What is mixed inhibitor?
Binds Allosteric site of enzyme and enzyme substrate complex Vmax decreases Km increases (ES) decreases (E)