Key notes

Question 1

Haemotoxin stain

Answer 1

binds acidic molecules

Question 2

Eosin stain

Answer 2

binds basic molecules

Question 3

How many bonds do A and T form

Answer 3

2

Question 4

How many bonds do G and C form

Answer 4

3

Question 5

B-DNA

Answer 5

classic helical structure

Question 6

A-DNA

Answer 6

more coiled than classic DNA structure

Question 7

Z-DNA

Answer 7

less coiled than classic DNA structure

Question 8

Origin of replication (prokaryotes)

Answer 8

OriC (one replicon)

Question 9

(replication)
DnaA

Answer 9

binds to 9mer region
recruits DnaB, DnaC, helicase and helicase loader

Question 10

RNA polymerase 1

Answer 10

pre r-RNA

Question 11

RNA polymerase 2

Answer 11

mRNA, SnRNA, miRNA

Question 12

RNA polymerase 3

Answer 12

tRNA, 5sRNA, SnRNA, 7sRNA

Question 13

Eukaryotic transcription factors

Answer 13

GC box
CAAT box
TATA box

Question 14

Lac operon

Answer 14

Lac Z - catalyses cleavage of lactose to glucose

Lac Y - transports lactose across membrane

Lac A - rids cells of toxic thiogalactosides

Question 15

Ribosome sites

Answer 15

A(aminoacyl), P(peptidyl), E(exit), mRNA binding

Question 16

Translation initiation site in prokaryotes

Answer 16

Shine-Dalgarno

Question 17

Translation initiation site in eukaryotes

Answer 17

Kozak sequence

Question 18

Function of polyA tail

Answer 18

binds to 5’ cap
makes it quicker for ribosomes to dissassemble at the end and reassemble

Question 19

Eupeptide bond

Answer 19

bond between Ca and a-Amino

Question 20

Isopeptide bond

Answer 20

bond between side chain and Ca or a-amino

Question 21

Amino acids most likely to be found in a-helix

Answer 21

Alanine
Methionine
Glutamate

Question 22

Amino acids most likely to be found in b-sheet

Answer 22

Tyrosine
Isoleucine
Valine

Question 23

Amino acids most likely to be found in b-turn

Answer 23

proline
glycine
asparagine

Question 24

Co-factor

Answer 24

molecule that is a part of the active site of an enzyme

ions
co-enzymes

Question 24

Co-enzyme

Answer 24

organic cofactors that assist enzymes in carrying out their catalytic function

Question 25

Holoenzyme

Answer 25

apoenzyme + cofactor

Question 26

Prosthetic group

Answer 26

Covalently bound coenzyme

Question 27

co-substrate

Answer 27

loosley bound co-enzyme

Question 28

apoenzyme

Answer 28

enzyme without its cofactor

Question 29

1. Oxidoreductase

Answer 29

Ared +Box -> Aox + Bred oxiation/reductions

Question 30

2. Transferase

Answer 30

AB + C -> A + BC transfer functional groups

Question 31

3. Hydrolase

Answer 31

AB + H2O -> A-H + B-OH transfer water

Question 32

4. Lyases

Answer 32

A=B + X-Y -> A(X)-B(Y) break chemical bonds without using water (hydrolysis) or oxidation-reduction reactions

Question 33

5. Isomerases

Answer 33

A -> B catalyse geometric and structural changes

Question 34

6. Ligases

Answer 34

Join molecules cause reduction of ATP to ADP

Question 35

7. Translocase

Answer 35

facilitate the movement of molecules, including proteins, ions, and smaller molecules, across cell membranes

Question 36

Menten assumptions

Answer 36

1. conversion of P to S is negligable 2. [ES] is constant at steady state 3.Vo = K2[ES] 4. [So] = [S] changes in S are negligable 5. [Eo] = [ES] + [E]

Question 37

Fed state

Answer 37

Brain: glucose Liver: uses excess fuel (glycogen and fat) Tissues: take up excess glucose (glycolosis) Adipose: breaks down glucose to store fat increased glycolisis inhibits fatty acid oxidation

Question 38

Fasting state

Answer 38

Brain: ketone bodies Liver: releases glucose (gluconeogenesis) Adipose: releases fatty acids Tissues: switch to fat use

Question 39

Excersizing

Answer 39

Muscle: fule use increases Adipose: releases fatty acids Liver: releases glucose