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

1
Q

What is the most abundant protein in human body

A

Type I Collagen

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2
Q

Collagen is a triple helix from which 3 amino acids?

A

Proline
Hydroxyproline
Glycine

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3
Q

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

A

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

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4
Q

Globular proteins are ______ in aqueous environments

A

Soluble

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5
Q

Name 2 examples of fibrous proteins

A

Collagen

Keratin

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6
Q

Name 1 disease caused by mutations in type I collagen

A

Osteogenesis imperfecta

Will lead to more bone fractures and collagen defects

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7
Q

Why will lack of vitamin C lead to scurvy?

A

Reduce proline converted to hydroxyproline

Less collagen formed, leading to scurvy

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8
Q

Name 3 locations with keratin

A

Hair
Skin
Nails

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9
Q

How many haem groups does haemoglobin have?

A

4

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10
Q

Myoglobin has how many haem groups

A

1

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11
Q

What is the function of myoglobin

A

Facilitates Oxygen diffusion in Muscles

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12
Q

What is the function of neuroglobins

A

Oxygen carrier in neurones

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13
Q

What’s meant by positive cooperativity

A

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

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14
Q

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

A

T state has lower affinity

R state has higher affinity

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15
Q

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

A

Lower

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16
Q

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

A

Higher

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17
Q

Name a molecule responsible for folding of proteins

A

Chaperone (HSP60)

18
Q

What are prions

A

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

19
Q

Name 2 diseases that prion will cause

A

Mad Cow Disease
CJD
Alzheimer Disease

20
Q

Name/ Describe the reactions that prion diseases will undergo

A

PrPc to PrPSc

21
Q

Prion disease reaction

PrPc to PrPSc will cause entire alpha helix to become some______

A

Beta sheets

22
Q

What are ddNTPs?

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

A

Nucleotides with both 2’ and 3’ deoxygenated

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

23
Q

What is the aim of DNA Sequencing

A

Work out the order of ACGT bases of the DNA molecules

24
Q

Sagner sequencing relies on _______

A

ddNTPs

25
Q

In Sagner Sequencing, short chains migrate quicker in ____________

A

Capillary Electrophoresis

26
Q

In Next Generation Sequencing, what is the advantage?

A

Quicker

27
Q

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

A

22 pairs of autosomes

1 pair of allosome

28
Q

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

A

Short (p) arm

Long (q) arm

29
Q

Name the 3 types of Genetic Variation

A
  1. Copy number variation (gain/loss of entire chromosomes)
  2. Structural variation
  3. Sequence level variation (Single nucleotide polymorphisms, single base change)
30
Q

ATP synthase contains which 2 units?

And, what are they

A

F0 unit: The C ring

F1 unit: The part with 3 alpha and 3 beta subunits

31
Q

The F1 unit contains 3 states, name them

Also, name their respective functions

A

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

32
Q

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

A

30 to 32

33
Q

Which enzyme is required for the Formation of Acetylcholine?

A

ChAT

34
Q

What enzyme is required for the degradation of Acetylcholine?

A

AChE

35
Q

Name 5 Ways to modify the enzyme to become active or inactive

And are they reversible

A
Phosphorylation- Reversible
Cleavage of Peptide Bonds- Irreversible
Add Activator or Inhibitor- Reversible
Allosteric regulator
Number of enzyme molecules
36
Q

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

A

Serine
Threonine
Tyrosine

37
Q

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

A

Allosteric Regulators

38
Q

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

A

Substrates

39
Q

Positive Allosteric Regulator means ___________

A

The enzyme is responding to a very low concentration of substrate more sensitively

(Basically, increase the rate of reaction)

40
Q

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

A

Holoenzyme (active)

41
Q

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

A

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