Class 1

Question 1

What is the primary structure of a protein?

Answer 1

Sequence of AAs

Question 2

What is the secondary structure of a protein?

Answer 2

H bonding between back bone

-helix, beta sheet

Question 3

What is the tertiary structure of a protein ?

Answer 3

Side chain interactions with a polypeptide

Question 4

What is the quaternary structure of a protein?

Answer 4

Side chain interaction between different polymers/groups of proteins

Question 5

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

Answer 5

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

these brake with acid/base, heat and salt solution

Question 6

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

Answer 6

disulphide bridges fir Cystein (cys) C

Question 7

How aree starch cellulose and glycogen all linked together?

Answer 7

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

beta 1,4 = cellulose

Question 8

What are carbs used for?

Answer 8

Energy
Cell surface markers
Adhesion

Question 9

What is a transfat?

Answer 9

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

Question 10

What are Triglycerides?

Answer 10

3 FA and a glycerol

Question 11

How are TGs made?

Answer 11

Dehydration synthesis

Forms ester bonds during synthesis

Question 12

What are terpenes?

Answer 12

Made from isoprene units (need at least 2)

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

Question 13

What is the structure of steroids and cholesterol ?

Answer 13

3 cyclohexane and 1 cyclopentane

Question 14

What does G, H and T and S mean?

Answer 14

G free energy
H Enthalpy
T temp
S entropy

Question 15

What happens when G is positive of negative?

Answer 15

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

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

Question 16

What does exergonic mean?

Answer 16

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

Question 17

Are transition states stable?

Answer 17

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

Question 18

Why are lower activation energies more stable?

Answer 18

Increases stabilization of transition state

Reduce activation energy

Question 19

Are enzymes. always on?

Answer 19

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

Question 20

What is allosteric regulation?

Answer 20

Regulate enzymes via conformation change

Question 21

What is a negative feedback?

Answer 21

Product inhibits something at the start of the chain

Question 22

What its a positive feedback?

Answer 22

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

Question 23

What does max depend on?

Answer 23

[Enzyme]

Type of enzyme you’re working with

Question 24

What is the Km?

Answer 24

Concentration of the substrate required to reach 1/2 Vmax

-the affinity it has for the substrate

Question 25

What happens when substrate affinity increases?

Answer 25

Km decreases

Question 26

What are the 4 kinds of inhibition?

Answer 26

Competition
Non competition
Uncompetitive
Mixed inhibitors

Question 27

What is competition inhibition?

Answer 27

Binds active site
Vmax is unchanged
Km: increases (low affinity)

Question 28

What is the non competition inhibition?

Answer 28

Binds allosteric site of enzyme
Vmax decreases
Km unchanged

Question 29

What is uncompetitive inhibition?

Answer 29

Binds allosteric site of enzyme substrate complex
Vmax decreases
Km decreases

Question 30

What is mixed inhibitor?

Answer 30

Binds Allosteric site of enzyme and enzyme substrate complex
Vmax decreases
Km increases (ES) decreases (E)