AAMC Test 1 set Flashcards
Cavernous
large cave or chamber
Critical point
point at which different phases of matter can exist simultaneously
Triple point
where solid, liquid, and gas can exist simultaneously
Phase boundary
transition point of matter
Bond formation
Bond formation is an exothermic process -> energy is release so -H
- Bond formation and bond breaking of the same atoms yield the same magnitude of energy but opposite signs
When matter is changing phase, it’s temperature is..
When matter is changing phase, it’s temperature is constant until the phase change is complete
Heat of vaporization
the amount of enthalpy added to a liquid to transform it into gas
Heat (or enthalpy) of fusion
amount of heat that is required to change a specific quantity of a substance from a solid to a liquid without increase in temperature and at constant pressure
Calorimetry
measure the transfer of heat in chemical reactions, physical changes, and phase changes
Electric fields
vector fields which have a magnitude and direction
- The direction of the magnetic field is the direction force will be exerted on a positive charge when placed in that field
A proton and electron are oppositely charged and will produce an attractive force on one another
- The attractive force experienced by each charge will be equal and opposite
- Acceleration of an object is equal to force/mass -> Due to the electron’s mass being smaller, it will experience a greater acceleration
To determine the magnitude of the acceleration that each charge experiences, we must know:
- Charge magnitude, charge mass, and distance between the charges
Coulomb’s Law
- F = k (q1q2/d^2)
-ase
protein enzyme
Enzymes that are not proteins
ribosome (made of RNA)
Catalyst/enzymes
lowers activation energy
- Vast majority of enzymes are reversible
Enzymes in glycolysis that are irreversible in physiological conditions:
Hexokinase (rxn 1), PFK (rxn 3), pyruvate kinase (rxn 10)
Vmax
maximum rate of enzyme activity - we never reach Vmax
- Asymptotic curve - curve gets closer but never reaches
Km
the amount of substrate required for the enzyme to work at 1/2 the maximum rate of enzyme
- The higher the km = the lower the affinity of the enzyme to the substrate
Hexokinase
high affinity, low kcat
Glucokinase
lower affinity high kcat
Kcat
catalytic rate- the max speed of one enzyme - how quickly can you work at maximum rate
Need enzymes with different affinities and efficiency to allow
Need enzymes with different affinities and efficiency to allow for adaptivity and balanced use of substrate throughout the body
Cooperative enzyme
Hill coefficient > +/-1
- E.g. hemoglobin - cooperatively binds to oxygen
Positive Hill coefficient = positive cooperativity = when binding of a ligand to an enzyme enhances the binding of additional ligand to that enzyme
Negative Hill Coefficient = negative cooperativity = when binding of a ligand to an enzyme inhibits the binding of additional ligand to that enzyme