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Energy - Coggle Diagram
Energy
Reaction rates
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for a rate of reaction the reactants must collide, be in the right orientation, have enough energy, collide in correct proportion
k=Ae^(-E/RT) (R=gas constant, T=temperature, E=activation energy
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Half lives
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first order
since looking for when [A]=1/2 [a] at t, so half life=ln(2)/k
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Thermodynamics
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Laws of thermodynamics
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Third Law
Entropy(S) is 0 when system is at absolute 0, and ways of arranging a molecules is 0
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Zeroth Law
if system A is in thermal equilibrium with B and B is in thermal equilibrium with C than A is in thermal equilibrium with C
entropy
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however, when the system contains water the protein folded has a higher entropy than the unfolded version
Free energy
Coupling reactions
direct coupling involves an enzyme with an active site that forces 2 different ligands together and a reaction to occur
glucose->glucose phosphate is positive free energy (so requires ATP becaseu ATP->ADP + Pi is largely negative)
calculation
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=RTln(concentration in/concentration out) x number of electrons x Faraday constant x voltage of membrane
Half reactions
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deltaE0 values are found in tables and measured relative to standard hydrogen electrode (said to be 0V but recalculated as -0.421V)
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the reactoion will drive all the reactions below it in revere, so reduction of oxygen for water drives all in reverse
example- pyruvate drives NADH in reverse (because pyruvate is above NADH (-0.185V to -0.32V) so deltaE0 is +0.135V which means deltaG0 is positive so favourable)
Measuring
Enthalpy
Bomb Calorimeter
force oxygen into bomb, using high pressure, containing the sample
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Energy (A+B->C)
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equilibrium dialysis
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over time the ligand concentration will become equal, and ligand will bind to protein so unbound ligand concentration is higher out of bag
this sets up concentration gradient, if ligand is charged the voltage diffrence can be measured
when reaction is favourable the free energy is negative which is an exergonic change (the reverse is endergonic change)
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