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
Q

sugar cube dissolved in a cup of coffee. what happens to entropy of the sugar?

A

it increases.

sugar cube dissolves, more freedom of movement/random movement; increased entropy (more disordered)

26
Q

what is the first law of thermodynamics?

A

energy can not be created or destroyed (law of conservation of energy)

states that energy can be transduced from one form to another

27
Q

ATP carries stored potential energy and transfers it through the formation of

A

phosphate bonds

28
Q

Reactions that have positive standard free energy changes (ΔG’°>0) can be made to occur in cells by:

A

both coupling them with exergonic reactions via a common intermediate and manipulating the concentrations of products and reactants such that ΔG’<0

29
Q

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)

A

standard conditions.
the concentrations of reactants and products.
the ratio of [ADP] / [ATP].
the temperature at which the cell is found.

30
Q

For a reaction with a standard free energy change, ΔG’° = +0.7 kcal/mole, how can we make the rxn occur?

A

The reaction could be made to occur by altering the concentrations of reactants and products