Thermodynamics Flashcards

1
Q

Thermodynamics

A

The study of energy and hot it is distributed

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2
Q

Gravitational potential =

A

Mass x height x acceleration

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2
Q

Energy

A

The capacity to do work

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3
Q

Thermal energy =

A

Heat capacity x temperature

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4
Q

First law of thermodynamics

A

The amount of energy within the universe is constant, energy cannot be created or destroyed (ALL energy came from bing bang)

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5
Q

Second law of thermodynamics

A
  • Descrbies the observation that energy moves from an area of high concentration to one of low concentration.

RULES:
1. Heat will spontaneously flow from a material at high temperature to a material at lower temperature
- Some heat energy is lost when energy is converted
- In an isolated system a process can occur only if it increases the total entropy of the system.
- Disorder in the universe tends to increase

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6
Q

Was the big bang low or high entropy

A

Low entropy - all energy in an infinitely small single point - infinitely ordered

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7
Q

Enthalpy

A

The energy required to form a system.

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7
Q

Change in enthalpy =

A

Enthalpy of formation
of product - Enthalpy of formation of reactants

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8
Q

How does life exist

A

By using energy to increase order (decrease entropy)

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9
Q

Change in Entropy =

A

Enthalpy of formation
of product - Enthalpy of formation of reactants

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10
Q

Gibbs free energy =

A

Enthapy - (Temperature x Entropy)

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11
Q

How do you know if a reaction is feasible

A
  • If ΔG is LESS than 0 the reaction will run forward
  • If ΔG is GREATER than 0 the reaction will run backwards
  • If ΔG is at 0 the reaction is at equilibrium
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12
Q

Activation energy

A

Energy required for a reaction to proceed, it controls how fast a reaction will reach equilibrium

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13
Q

How does biology get unfavourable reaction to work? Example…

A
  1. Calcium pump, uses ATPase to make calcium go against its concentration gradient
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14
Q

What do enzymes do

A

Enzymes increase the rate of reaction by reducing the activation energy of a reaction, BUT do not change the equilibrium for a reaction

15
Q

Substrate binding

A

Held in place by
- Hydrogen bonds
- Ionic bonds
- Hydrohpobic interactions

16
Q

Lock and key model

A

Substrate is complimentary to the active site

17
Q

Induced fit

A

The enzyme and substrate bind and undergo a change in conformation and stabilise the transition state and reduce the activation energy so the reaction can proceed.

18
Q

Negative delta G name

19
Q

Negative delta G name

A

Endergonic

20
Q

Enzyme promiscuity

A

Enzymes can have different reactions

21
Q

Broad specificity

A

Same reaction different substrate leads to different product

22
Q

Methods for measuring concentration of substrate or product

A
  1. Colour
    Substrates and products can have a colour. Eg. In the reaction with NITROCEFIN the susbtrate is yellow and the product is red.
    You can also use a spectrophotometer to measure the absorption of ultraviolet light, eg NADH and FADH absorb a specific wavelength of light
  2. Catalase reaction
    measuring the change in state going from liquid to gas so testing if the gas is present
  3. Size
    Some enzymes alter the size of substrates. Eg DNA restriction endonuclease breaks down DNA
23
Vmax
V = Rate so Maximal rate Always slightlty above where the curve platues
24
Km
Machaelis constant, Affinity of the enzyme for the substrate. Its = to half the Vmax. The smaller the Km the better the bonding and the larger the Km the stronger the bonding.
25
Michaelis Menton equation
V = Vmax [S]/Km+[S]
26
Pros of Michaelis equation
- It tells you the Km - it tells you the Vmax Can be used to tell you how well an enzyme works after mutation, eg may affect the Vmax but no the substrate concentration (Km)
27
Cons of Michaelis equation
- It is very hard to plot by hand accurately so the equation can be changed for simpler plotting. Can be rearranged into y=mx+C form - 1/V = Km/Vmax x 1/[s] +1/Vmax which gets a linear line
28
Eadie-hofstee
v=-kmxv/[s]+Vmax Km = Slope Vmax = y intercept
29
Hanes Woolf
[s]/v=[s]/Vmax + Km/Vmax
30
How does competitive inhibitors affect vmacx and km
Doesnt impact vmax only impacts km (increasers as worse bonding)
31
How does an inhibitor affect the Michaelis menton equation
slower rate so curve under original
32
Ki
the concentration of an inhibitor at which the reaction rate is half of the vmax.
33
Ki and drugs
Provides you info on how active a drug will be. The lower the Ki the moer effective the drug is at inhibiting the enzyme Eg. Acetyl choline esterase, releases