IASM 08 09 11 14: Protein, ATP, Enzymes, Precision Medicine

Question 1

What is the most abundant protein in human body

Answer 1

Type I Collagen

Question 2

Collagen is a triple helix from which 3 amino acids?

Answer 2

Proline
Hydroxyproline
Glycine

Question 3

In collagen: Each individual strand is ______ helix, while combined it is ________ helix

Answer 3

individual: left-handed alpha helix
Combined: Right-handed Super helix

Question 4

Globular proteins are ______ in aqueous environments

Answer 4

Soluble

Question 5

Name 2 examples of fibrous proteins

Answer 5

Collagen

Keratin

Question 6

Name 1 disease caused by mutations in type I collagen

Answer 6

Osteogenesis imperfecta

Will lead to more bone fractures and collagen defects

Question 7

Why will lack of vitamin C lead to scurvy?

Answer 7

Reduce proline converted to hydroxyproline

Less collagen formed, leading to scurvy

Question 8

Name 3 locations with keratin

Answer 8

Hair
Skin
Nails

Question 9

How many haem groups does haemoglobin have?

Answer 9

4

Question 10

Myoglobin has how many haem groups

Answer 10

1

Question 11

What is the function of myoglobin

Answer 11

Facilitates Oxygen diffusion in Muscles

Question 12

What is the function of neuroglobins

Answer 12

Oxygen carrier in neurones

Question 13

What’s meant by positive cooperativity

Answer 13

The affinity to oxygen is higher when there’s more oxygen molecules bound to the haemoglobin

Question 14

Compare T state and R state, which has lower and higher affinity to Oxygen?

Answer 14

T state has lower affinity

R state has higher affinity

Question 15

Oxygen has ______ affinity to haemoglobin in lower oxygen concentration (e.g. tissues)

Answer 15

Lower

Question 16

Oxygen has ______ affinity to haemoglobin in higher oxygen concentration (e.g. lungs)

Answer 16

Higher

Question 17

Name a molecule responsible for folding of proteins

Answer 17

Chaperone (HSP60)

Question 18

What are prions

Answer 18

Misfolded proteins that become catalysts, they induce normal proteins to become misfolded proteins

Question 19

Name 2 diseases that prion will cause

Answer 19

Mad Cow Disease
CJD
Alzheimer Disease

Question 20

Name/ Describe the reactions that prion diseases will undergo

Answer 20

PrPc to PrPSc

Question 21

Prion disease reaction

PrPc to PrPSc will cause entire alpha helix to become some______

Answer 21

Beta sheets

Question 22

What are ddNTPs?

Nucleotides with both _________________
So it cannot continue the chain by binding to the next nucleotide molecule

Answer 22

Nucleotides with both 2’ and 3’ deoxygenated

So it cannot continue the chain by binding to the next nucleotide molecule

Question 23

What is the aim of DNA Sequencing

Answer 23

Work out the order of ACGT bases of the DNA molecules

Question 24

Sagner sequencing relies on _______

Answer 24

ddNTPs

Question 25

In Sagner Sequencing, short chains migrate quicker in ____________

Answer 25

Capillary Electrophoresis

Question 26

In Next Generation Sequencing, what is the advantage?

Answer 26

Quicker

Question 27

Human genome has 22 pairs of _______ and 1 pair of ________.

Answer 27

22 pairs of autosomes | 1 pair of allosome

Question 28

The short arm of DNA is referred to as ____ arm and the long arm of DNA is referred to as ____ arm

Answer 28

Short (p) arm | Long (q) arm

Question 29

Name the 3 types of Genetic Variation

Answer 29

1. Copy number variation (gain/loss of entire chromosomes) 2. Structural variation 3. Sequence level variation (Single nucleotide polymorphisms, single base change)

Question 30

ATP synthase contains which 2 units? | And, what are they

Answer 30

F0 unit: The C ring | F1 unit: The part with 3 alpha and 3 beta subunits

Question 31

The F1 unit contains 3 states, name them | Also, name their respective functions

Answer 31

Loose State: ADP and P binds loosely Tight State: ADP and P binds tightly Open State: Allows ATP to leave and ADP, P to enter

Question 32

How many ATP molecules can be produced from 1 glucose molecule?

Answer 32

30 to 32

Question 33

Which enzyme is required for the Formation of Acetylcholine?

Answer 33

ChAT

Question 34

What enzyme is required for the degradation of Acetylcholine?

Answer 34

AChE

Question 35

Name 5 Ways to modify the enzyme to become active or inactive And are they reversible

Answer 35

``` Phosphorylation- Reversible Cleavage of Peptide Bonds- Irreversible Add Activator or Inhibitor- Reversible Allosteric regulator Number of enzyme molecules ```

Question 36

In enzyme phosphorylation, the phosphate group can be added to which amino acids?

Answer 36

Serine Threonine Tyrosine

Question 37

The regulatory unit of the enzyme is responsible for binding to __________

Answer 37

Allosteric Regulators

Question 38

The catalytic unit of the enzyme is responsible for binding to ______

Answer 38

Substrates

Question 39

Positive Allosteric Regulator means ___________

Answer 39

The enzyme is responding to a very low concentration of substrate more sensitively (Basically, increase the rate of reaction)

Question 40

After adding a co-enzyme, an apoenzyme (inactive) becomes a ________ (___)

Answer 40

Holoenzyme (active)

Question 41

Some examples of coenzymes, what are they for? Vitamin B12 Vitamin B5 VItamin B6

Answer 41

B12-Fatty acid oxidation and synthesis B5-Glucose metabolism B6-Glycogen metabolism