lecture 4 Flashcards

1
Q

negative delta G

A

spontaneous rxn

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2
Q

how can unfavourable rxns occur?

A

if they are coupled to a favourable one

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3
Q

for sequential rxns, standard free energy changes are

A

additive

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4
Q

the free energy is directly related to

A

the ratio of concentration of product and reactants

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5
Q

activation energy (Ea)

A

energy must be acquired by a molecule to undergo a chem rxn

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6
Q

what does delta G not tell us?

A

the speed of rxn

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7
Q

catalyst

A

lowers Ea of a rxn

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8
Q

Enzyme

A

biological catalyst. speeds up rxn rate by lowering Ea

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9
Q

Enzymes are

A

-not consumed in the process
-highly specific in terms of substate and rxn
-allow rxns to occur quickly

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10
Q

does delta G change w time?

A

yes, bc the concentration of products and reactants is changing

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11
Q

steady state equilibrium

A

relatively stable equilibrium. concentration of products and reactants vary slightly

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12
Q

are cells ever at a thermodynamic equilibrium?

A

no! unless dead

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13
Q

living cells are constantly exchanging

A

material with their environment

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14
Q

equilibrium constant

A

the ratio of substrates and product when the rates of the forward and reverse rxns are equal

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15
Q

equilibrium constant (K=?)

A

[products]/[reactants]

assume delta G is zero if not given

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16
Q

A + B –><– AB
if A and B bind non-covalently, is the free energy change positive or negative?

A

Negative bc rxn is favourable

-if A and B bind strongly, you need less of A and B to make product

17
Q

chemical siphons

A

drives energetically unfavourable rxns

18
Q

thermal motion

A

-molecules diffuse
-larger molecules diffuse slower than small ones
-random encounters between substrate and enzyme can lead to formation of an enzyme-substrate complex stabilized by noncovalent interactions

19
Q

enzyme kinetics: velocity

A

rate of rxn

20
Q

Vmax

A

the max velocity of a rxn for an enzyme. how quickly it can catalyze a rxn when fully saturated w substrate

21
Q

Michaelis constant (Km)

A

concentration of substrate at which enzyme is at half Vmax

22
Q

entropy

A

measure of a system’s disorder

23
Q

do competitive enzymes bind reversibly or irreversibly to the substrate?

A

reversibly

24
Q

turnover number for an enzyme definition

A

the maximum number of molecules of substrate that can be converted to product by one enzyme molecule per unit time

25
sugar cube dissolved in a cup of coffee. what happens to entropy of the sugar?
it increases. sugar cube dissolves, more freedom of movement/random movement; increased entropy (more disordered)
26
what is the first law of thermodynamics?
energy can not be created or destroyed (law of conservation of energy) states that energy can be transduced from one form to another
27
ATP carries stored potential energy and transfers it through the formation of
phosphate bonds
28
Reactions that have positive standard free energy changes (ΔG'°>0) can be made to occur in cells by:
both coupling them with exergonic reactions via a common intermediate and manipulating the concentrations of products and reactants such that ΔG'<0
29
To predict the direction in which a particular reaction will proceed at a given moment within a particular cellular compartment, one must know all of the following (4)
standard conditions. the concentrations of reactants and products. the ratio of [ADP] / [ATP]. the temperature at which the cell is found.
30
For a reaction with a standard free energy change, ΔG'° = +0.7 kcal/mole, how can we make the rxn occur?
The reaction could be made to occur by altering the concentrations of reactants and products