BCH 361 EXAM 2 QUESTIONS WITH ALL VERIFIED ANSWERS
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BCH 361 EXAM 2 QUESTIONS WITH ALL VERIFIED ANSWERS
The DNA in each human cell if connected and fully extended will be meters long. - Answer-2
Supercoiling accounts for some of the compaction of the DNA, but further compaction occurs by to the DNA. - Answer-binding certain proteins
chromatin...
BCH 361 EXAM 2 QUESTIONS WITH
ALL VERIFIED ANSWERS
The DNA in each human cell if connected and fully extended will be meters long. -
Answer-2
Supercoiling accounts for some of the compaction of the DNA, but further compaction
occurs by to the DNA. - Answer-binding certain proteins
chromatin - Answer-is the entire complement of a cell's DNA and its associated
proteins.
histones - Answer-are highly basic proteins that are components of chromatin.
Histones (an octamer that contains two copies of H2A, H2B, H3, H4) and of
DNA comprise a . - Answer-200 bp ; nucleosome
Nucleosomes are joined by (~ 70 bp long) , to which binds, so that the
histone-DNA complex has the appearance of beads on a string. - Answer-linker DNA ;
H1 binds
Digestion of the linker DNA yields the . - Answer-nucleosome core
particle
***DNA wraps around the histone octamer twice to form the nucleosome core particle.
The of the core particle are arranged as an . DNA wraps around the
outside of the octomer. - Answer-eight histones ; octamer
Nucleosomes themselves are arranged in a (36 nm fibers) that further
compacts the DNA. - Answer-helical array
Why are supercoiling and nucleosome formation important for the structure of DNA in
the cell - Answer-Both supercoiling and nucleosome formation help to compact the
DNA
What is the purpose of the oxyanion hole in chymotrypsin? - Answer-The oxyanion hole
is a structure at the active site of chymotrypsin that stabilizes the tetrahedral
intermediate in the proteolysis reaction and facilitates the formation of the acyl-enzyme
intermediate.
What caused a "burst" of activity followed by a steady-state reaction when chymotrypsin
was studied in the milliseconds subsequent to mixing the enzyme and substrate? -
Answer-Chymotrypsin cleaves peptide bonds in a two-step reaction, in which the first
step, the formation of the acyl-enzyme intermediate, is faster than the second step,
hydrolysis.
If chymotrypsin is such an effective protease, why doesn't it digest itself? - Answer-
Chymotrypsin recognizes large hydrophobic groups, which are usually buried in the
,enzyme's core owing to the hydrophobic effect.
Covalent Catalyst - Answer-the active site is briefly covalently modified.
acid bas catalyst - Answer-an amino acid residue at the active site of the enzyme
donates or accepts a proton.
metal ion catalyst - Answer-metal ion (+1, +2, +3) cofactors
Catalysis by approximation and orientation - Answer-the enzyme brings two substrates
together in an orientation that facilitates reaction.
What kind of catalyst do amino acid residues participate in? - Answer-acid base catalyst
these include: glutamate, Asparatate, lysine, arginine, cysteine, histidine, serine,
tyrosine
Metal ion catalyst may... (4 points) - Answer-act as an electrophilic catalyst in reduction-
oxidation reactions,
stabilizing a negative charge on the reaction intermediate,
increase the acidity of a nearby molecule,
increase the binding energy with substrate.
Temperature enhances the rate of enzyme catalyzed reactions, however, too high
temperature causes what - Answer-denaturation of the enzyme
Tyrosinase is an enzyme that catalyze the - Answer-black pigment formation.
EX: cat that has some black pigment but mostly white has a low tolerant to heat
, Enzymes isolated from thermophilic archaea are very important biochemical and
bioengineering tools as they have very good - Answer-resistance to high temperatures
The optimal pH of an enzyme varies but it is correlated with what? - Answer-the
environment of the enzyme
Two types of inhibition in terms of reversibility: - Answer-reversible inhibition and
irreversible
Three types of reversible inhibition - Answer-Competitive inhibition
Uncompetitive inhibition
Noncompetitive inhibition
They differ by the modes of inhibitor-enzyme interactions and the changes of the
enzyme kinetics.
Competitive Inhibitor binds - Answer-to the same site as the substrate thus excludes the
substrate.
Uncompetitive inhibitor binds to - Answer-the enzyme-substrate complex to form a
tertiary complex (E-S-I) which cause the enzyme to lose its activity.
noncompetitive inhibitor binds to - Answer-the enzyme at a different site from the
substrate, both to the E or ES, that affect the activity.
In competitive inhibition what happens to Km and Vmax - Answer-KM is increased in the
presence of inhibitor. (as the Inhibitor pulls the ES equilibrium backward)
Vmax of the enzyme is unchanged. The inhibition can be overcome by a sufficiently
high concentration of substrate (as the inhibitor will be displaced).
In competitive inhibition what happens with higher [I] and [S]? - Answer-Higher [I] shifts
the kinetic curve to the right.
Sufficiently high [S] can completely relieve competitive inhibition to reach the same
Vmax.
Is product formed in uncompetitive inhibition? - Answer-In uncompetitive inhibition, the
enzyme-inhibitor-substrate ternary complex does not form product.
What happens to Vmax and Km in uncompetitive inhibition? - Answer-Consequently, in
the presence of uncompetitive inhibitor, Vmax is lower and the KM is also lower
(Inhibitor drives the ES equilibrium forward)
Uncompetitive inhibition cannot be overcome by the addition of excess substrate.
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