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Altius 1 MCAT Practice Exam with Accurate Solutions

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Altius 1 MCAT Practice Exam with
Accurate Solutions

Pt - ANSWER-platinum

Pd - ANSWER-palladium

Deuteration - ANSWER-heavy water, D2O

on a pH titration curve, the buffering capacity is along which lines - ANSWER-horizontal

What does Hydrophobic interaction chromatography (HIC) depend on - ANSWER-salt
concentration

direction of electrons and current - ANSWER-opposite

electrons flow from __ to __ - ANSWER-Negative (-) to Positive (+)

current flows from __ to __ - ANSWER-positive terminal to negative terminal

390 nm color - ANSWER-violet

700 nm - ANSWER-red

gamma rays - ANSWER-0.0001 nm to 0.01 nm

x-rays - ANSWER-0.01 nm to 10 nm

ultraviolet rays - ANSWER-10 nm to 400 nm

infrared - ANSWER-1000 nm to 0.1 cm

radio waves - ANSWER-1 cm to 1 m

is it cis or trans isomers that can stack closely to one another? - ANSWER-trans, which
means they can also have a higher bp

m/z - ANSWER-mass to charge ratio: best way to separate ions in a mass
spectrometer. this number is calculated by dividing the weight of the ion by its charge

, mass spectrometer - ANSWER--involves the ionization and fragmentation of
compounds; these fragments are then run through a magnetic field, which separates
them by mass to charge ration
-the total molecular weight can thus be determined, or the relative concentrations of the
different fragments can be calculated and compared against reference values to identify
the compound

Faraday collectors - ANSWER-metal cup designed to catch charged particles in a.
vacuum

what state is compound in for mass spectrometers - ANSWER-gaseous

how is sample ionized in mass spectrometry - ANSWER-bombarded by electrons from
a filament

In mass spec, the biggest number indicates...j - ANSWER--the biggest size which is the
size of the intact isomer
-the more of the intact isomer there is, the more stable it is

In mass spec, which bonds are typically not broken? - ANSWER-double bonds

Induced-fit mechanism - ANSWER-the enzyme stabilizes the transition state of the
substrate, causing a reduction in the activation energy of the transition state.

lock and key mechanism - ANSWER-the unchanged substrate is stabilized, not the
transition state

Michaelis-Menten equation - ANSWER-V0 = Vmax[S]/([S]+Km)

Km - ANSWER--michaelis constant
-measure of affinity of the enzyme for its substrate

higher km - ANSWER-lower affinity for its substrate because it requires a higher
substrate concentration to be half-saturated

can the km of an enzyme-substrate complex be altered? - ANSWER-no, its an intrinsic
property

kcat - ANSWER--measures the number of substrate molecules "turned over" or
converted to product, per enzyme molecules per second
-values between 101 and 103

vmax and kcat equation - ANSWER-vmax = [E]kcat

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