IASM 08 09 11 14: Protein, ATP, Enzymes, Precision Medicine Flashcards
What is the most abundant protein in human body
Type I Collagen
Collagen is a triple helix from which 3 amino acids?
Proline
Hydroxyproline
Glycine
In collagen: Each individual strand is ______ helix, while combined it is ________ helix
individual: left-handed alpha helix
Combined: Right-handed Super helix
Globular proteins are ______ in aqueous environments
Soluble
Name 2 examples of fibrous proteins
Collagen
Keratin
Name 1 disease caused by mutations in type I collagen
Osteogenesis imperfecta
Will lead to more bone fractures and collagen defects
Why will lack of vitamin C lead to scurvy?
Reduce proline converted to hydroxyproline
Less collagen formed, leading to scurvy
Name 3 locations with keratin
Hair
Skin
Nails
How many haem groups does haemoglobin have?
4
Myoglobin has how many haem groups
1
What is the function of myoglobin
Facilitates Oxygen diffusion in Muscles
What is the function of neuroglobins
Oxygen carrier in neurones
What’s meant by positive cooperativity
The affinity to oxygen is higher when there’s more oxygen molecules bound to the haemoglobin
Compare T state and R state, which has lower and higher affinity to Oxygen?
T state has lower affinity
R state has higher affinity
Oxygen has ______ affinity to haemoglobin in lower oxygen concentration (e.g. tissues)
Lower
Oxygen has ______ affinity to haemoglobin in higher oxygen concentration (e.g. lungs)
Higher
Name a molecule responsible for folding of proteins
Chaperone (HSP60)
What are prions
Misfolded proteins that become catalysts, they induce normal proteins to become misfolded proteins
Name 2 diseases that prion will cause
Mad Cow Disease
CJD
Alzheimer Disease
Name/ Describe the reactions that prion diseases will undergo
PrPc to PrPSc
Prion disease reaction
PrPc to PrPSc will cause entire alpha helix to become some______
Beta sheets
What are ddNTPs?
Nucleotides with both _________________
So it cannot continue the chain by binding to the next nucleotide molecule
Nucleotides with both 2’ and 3’ deoxygenated
So it cannot continue the chain by binding to the next nucleotide molecule
What is the aim of DNA Sequencing
Work out the order of ACGT bases of the DNA molecules
Sagner sequencing relies on _______
ddNTPs
In Sagner Sequencing, short chains migrate quicker in ____________
Capillary Electrophoresis
In Next Generation Sequencing, what is the advantage?
Quicker
Human genome has 22 pairs of _______ and 1 pair of ________.
22 pairs of autosomes
1 pair of allosome
The short arm of DNA is referred to as ____ arm and the long arm of DNA is referred to as ____ arm
Short (p) arm
Long (q) arm
Name the 3 types of Genetic Variation
- Copy number variation (gain/loss of entire chromosomes)
- Structural variation
- Sequence level variation (Single nucleotide polymorphisms, single base change)
ATP synthase contains which 2 units?
And, what are they
F0 unit: The C ring
F1 unit: The part with 3 alpha and 3 beta subunits
The F1 unit contains 3 states, name them
Also, name their respective functions
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
How many ATP molecules can be produced from 1 glucose molecule?
30 to 32
Which enzyme is required for the Formation of Acetylcholine?
ChAT
What enzyme is required for the degradation of Acetylcholine?
AChE
Name 5 Ways to modify the enzyme to become active or inactive
And are they reversible
Phosphorylation- Reversible Cleavage of Peptide Bonds- Irreversible Add Activator or Inhibitor- Reversible Allosteric regulator Number of enzyme molecules
In enzyme phosphorylation, the phosphate group can be added to which amino acids?
Serine
Threonine
Tyrosine
The regulatory unit of the enzyme is responsible for binding to __________
Allosteric Regulators
The catalytic unit of the enzyme is responsible for binding to ______
Substrates
Positive Allosteric Regulator means ___________
The enzyme is responding to a very low concentration of substrate more sensitively
(Basically, increase the rate of reaction)
After adding a co-enzyme, an apoenzyme (inactive) becomes a ________ (___)
Holoenzyme (active)
Some examples of coenzymes, what are they for?
Vitamin B12
Vitamin B5
VItamin B6
B12-Fatty acid oxidation and synthesis
B5-Glucose metabolism
B6-Glycogen metabolism
