lecture 3 - bioenergetics Flashcards

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1
Q

what is the dissociation constant? (Kd)

A

the reciprocal of the equilibrium constant (Kd = 1/Keq); how tightly a protein binds to its ligand

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2
Q

the lower the Kd…

A

the higher the binding affinity and the tighter the binding of a ligand to its receptor; the lower the ligand concentration needed to reach 50 percent of binding

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3
Q

allostery

A

binding of a molecule at one site on a macromolecule can change the three-dimensional shape of a distant site

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4
Q

exergonic

A

energy-releasing; products contain less energy than the reactants, occurs spontaneously

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5
Q

endergonic

A

energy-absorbing; products contain more energy than the reactants, not spontaneous

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6
Q

if delta G is negative…

A

the forward reaction (formation of products) will occur spontaneously, energy will be released

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7
Q

if delta G is positive…

A

the forward reaction will NOT occur spontaneously, energy must be added

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8
Q

if delta G is zero…

A

both forward and reverse reactions will occur; equilibrium

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9
Q

an exothermic reaction in which entropy increases…

A

occurs spontaneously

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10
Q

an endothermic reaction occurs spontaneously if…

A

entropy increases enough so the term can overcome the positive delta H

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11
Q

do enzymes alter the value of delta G?

A

no; they alter the activation energy

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12
Q

what does the velocity at which products are generated depend on?

A

the concentration of material in the transition state

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13
Q

the higher the activation energy…

A

the lower the fraction of reactants that reach the transition state, and the slower the overall rate of reaction

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14
Q

what does lowering the activation energy mean?

A

decreasing the difference in free energy between the reactants and the transition state

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15
Q

what does lowering activation energy result in?

A

acceleration of overall reaction rate

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16
Q

how can endergonic reactions occur spontaneously?

A

by coupling the reaction with another energy-releasing reaction to result in a negative delta G

17
Q

example of energy-releasing reaction?

A

hydrolysis of ATP (-7.3 kcal/mol)

18
Q

what type of bond contains useful energy in ATP molecule?

A

covalent bond; phosphodiester bonds

19
Q

ligand

A

the molecule to which a protein binds

20
Q

the stronger the interaction between a protein and ligand…

A

the lower the value of Kd

21
Q

Michaelis-Menten enzyme-substrate-binding hypothesis

A

the rate of an enzymatic reaction was proportional to the substrate concentration at low substrate concentrations, but at high substrate concentrations, the rate reached a plateau (Vmax)

22
Q

Michaelis constant (Km)

A

measure of the affinity of an enzyme for its substrate

23
Q

what does the Km indicate?

A

the substrate concentration that yields a half-maximal reaction rate (1/2Vmax)

24
Q

the smaller the value of Km…

A

the more effective the enzyme is at making product from smaller concentrations of substrate and the lower the substrate concentration needed to reach half-maximal velocity

25
Q

competitive inhibition

A

Vmax stays the same, Km increases

26
Q

noncompetitive inhibition

A

Vmax decreases, Km stays the same

27
Q

3 amino acids that can be phosphorylated

A

serine, threonine, tyrosine