Science Quiz / GU MCP Lectures 7,8,9

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Can you name the GU MCP Lectures 7,8,9?

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Lineweaver-Burk is also called a ______ ______ plot
at very low [S], the effects of a __________ inhibitor become negligible
Catalyst does not change __
_________ temperature = greater contribution of entropy
If a catalyst decreases the activation energy by a factor of 2, it increases the reaction rate by a factor of ____
“missing a component,” polypeptide part of the enzyme without its co-factor
when Keq < 1, ∆G is __________
Binds ES complex and free enzyme
K_D indicates __________ and is part of ____
the presence of an _______ is accounted for by α which is calculated by with the equation α = 1 + [I]/KI.
________ regulation will always have a “negative” effect on the reaction rate (slow the kinetics), ________ regulation can result in both positive and negative effects
inactive precursor that needs to be activated by a proteolytic step ex. zymogen
Primary structure of a protein has low entropy because it is forcing _______ to be more _________
energy barrier between the reactants and products
A‡(rate k1) is of higher energy than I‡ (rate k2) , making k_ the slower step
equation for entropy with Boltzmann's
number of times per sec an enzyme makes a product
Relaxed: more active state; higher affinity for the ________
An uncompetitive inhibitor binds ONLY to the___ ______
_____ inhibitors generate a complex pattern on a Lineweaver- Burk plot, with the _________ component affecting apparent KM and the _________ component affecting both KM and Vmax
____∆H = enthalpically favored
A catalyst lowers activation energy but more specifically, it does this by lowering the_____ _____ of the _____ _____
For uncompetitive inhib, Vmax is also ________ because the _____ ______ concentration available is decreased.
w is work done by the _______ on its __________
Efficient enzymes are described as approaching the_______-_______ limit because the rate of the enzyme bumping into the substrate is controlled by diffusion, which affects the chan
When ∆U=0, ΔS > or =
______ regulation is distinct from inhibitory regulation -- refers to a non-substrate regulator binding to a location distant from the active site of the enzyme.
The magnitude of lowering activation energy, ΔΔG‡, is proportional to the degree of rate ___________
___________ inhibitor decreases the catalytic activity of the enzyme without affecting its affinity for substrate
high-energy molecules (glucose), which would otherwise rapidly break down into their simpler, low-energy constituents (e.g. _____ and _____).
Spontaneous only at T>∆H/∆S, ____∆H and ____ ∆S
dissolving urea is an _______ reaction
The lines of a competitive inhibitor plot meet at the ___ _____
although uncompetitive inhib. lower KM, the overall effect is________ (Vmax decreases), since the ES complex is subsequently being “sopped up” by the uncompetitive inhibitor.
Tense: less active state; higher affinity for the _________
U P V (denoted by uppercase letters) represent ________ _________ which mean they are independent of _______
____∆G will do work on the surroundings
Formula for K_D =
∆G˚=∆G_f˚_____ of _______ - ∆G_f˚_____ of _______
when ∆U=0,
Mixed inhibition always decreases ______ but may increase or decrease ______
For mixed inhibition plot, when α =α’ lines meet at ___ ______
Enzymes are good for reactions in physiological conditions because they allow for _____ reaction conditions
kcat, or the _______ number, which is the number of times the enzyme turns over and does its job again per unit time
The high specificity of enzymes for their substrates, described by their KMs, means that enzyme catalyzed reactions rarely have non-productive _______ _______
Some transition state analogs bind _____ ______ than actual transition state meaning they bind at a _____ Km
The complexity of enzymes allows for multiple additional layers of ________
The experimental advantage of measuring ____ is that product inhibition and the reverse reaction are less likely to complicate measurements.
An otherwise endergonic reaction can be coupled to an exergonic reaction such as ______ ________
α (or α’) combines _______ of the inhibitor and its ______ for the enzyme
A protein folds into secondary and tertiary structures in order to maximize the _________ of _________
Spontaneous reactions go in the direction of ______ free energy
_____km = more efficient enzyme
Two steps: ________ substrate binding to enzyme and __________ formation of products from ES complex
competitive inhibitor is a substance that competes with the substrate for binding to the _______ binding site on the enzyme.
Living systems are _______ systems
_______ ________ _______ chemical compounds with a chemical structure that resembles the transition state of a substrate molecule in an enzyme-catalyzed chemical reaction
“ready to go,” (apoenzyme + cofactor)
_____ ______ concentration = [E]T
Energy (U) cannot be created nor can it be destroyed: ______ law of Thermodynamics
Km has units of ________
They are supposed to be as efficient as ________ to correctly do their job in an organism.
A system may attain order at the expense of ____________ its _____________
The initial velocity (v0) is defined as the velocity that is achieved when less than ____% of the ________ have been consumed.
The relationship between ΔG‡ and the reaction rate (k) is ______and ____________ (i.e. the higher ΔG‡, the _______ the rate (__)).
The universe tends towards maximum disorder: ______ law of Thermodynamics
_________: Transfer of electrons or protons (hydride ions or H atoms)
The _____ ______ ______ puts forth that after a rapid transient phase of the reaction, [__] remains essentially unchanged until nearly all of the reactants are consumed.
Enzymes include _______ binding sites or pockets which overlap with their _____ sites, where the chemistry of catalysis occurs. In some cases this overlap may be 100%
Slope (m) Lineweaver-Burk Plot=
____ = k2 [E]T
Enzymes do not alter ___________
The _________ of the Michaelis-Menineton ________ is a line known as the Double-Reciprocal or Lineweaver-Burk Plot
_________: Transfer of functional groups to water – enzymes that hydrolyze bonds by using water as the _______
The primary goal of many drugs that target enzymes is to _______ or _______ the activity of enzymes.
___________ inhibitor lowers both the apparent KM and Vmax, but KM/Vmax, the slope of the lines, remains ______
_________: Group-transfer reactions to another ______. Examples: methyl-transferase or phosphoryl-transferases (a.k.a.______)
_________ catalyze the formation of C-C, C-S, C-O, and C-N bonds that never existed before by ________ reactions coupled to ATP cleavage (Condensation opposite of ________)
For mixed inhibition, the inhibitor does not necessarily have the same KD for each type so it may have a higher affinity for binding to either the_____ ______ or the___ _______
inorganic ions, complex organic, metalloorganic molecules (ex. heme group)
the X intercept is _____
The Y intercept is ______
H= ___ + ___
The diagnostic Lineweaver-Burk plot for uncompetitive inhibition consists of a series _______ lines
Competitive inhibitor ___________ apparent Km
In uncompetitive, the enzyme and ________ can create the ES complex without a problem, but I binds to ES and creates an ________ ____ complex with a rate KI’
When V_0=1/2Vmax, Km= [__]
_________: Addition of groups to double bonds, or formation of double bonds by group removal (____ or _____ double bonds)
Although the reaction will never actually reach Vmax, it will get close enough where the ______ ______ extend beyond the Vmax line. At this point it is impossible to tell if the ve
k_cat represents _______ _______
_______ kcat/km= greater catalytic efficiency
_____ ______ is actually a transferase
____ ∆S = entropically favored
Formula for Km
Molecules that react with an enzyme irreversibly and decrease its activity are called ___________
Move group to another location on the same molecule to yield isomeric forms
A plot of 1/ ___ versus 1/[__] yields a straight line with the slope ________
All ________ systems must reach equilibrium
catalysts accelerate the process of reaching Keq, but do not ____ Keq.
q is heat absorbed by the _______ from the ___________
_____kcat means more efficient enzyme
____∆S = entropically opposed
Proenzymes, Coenzymes, Apoenzymes and Holoenzymes
large Keq, ∆G is _______
The rate of ___________ is inversely proportional to the change in _________ energy (ΔG‡) and is exponential
a ______ Km and a _____ kcat are each associated with a more efficient enzyme.
Km = [S] when ____ = ½ Vmax.
________ energy, ΔG‡, which represents the energy of a fleeting “______ state” between the substrate and products.
____ is expected to occur when the enzyme is completely saturated with substrate ([E]T = [ES]).
_______ is a measure of catalytic efficiency.
For uncompetitive inhib., apparent Km is _________ because _______ is ________, but it is inactive so it does NOT indicate that the enzyme is more efficient.
A substrate-analog that binds irreversibly to amino acids, usually the catalytic amino acid, thereby blocking the active site of the enzyme to other molecules and effectively 'kil
____∆G is only achieved if the surroundings do work on the reaction

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