Which force are involved in maintaining the primary structure of a
protein?
Covalent Bonds
1) Which
one is NOT an example of supersecondary structure?
A) The
pyrrole ring
B) The
greek key
C) The
beta meander
D) The
beta barrel
A. The pyrolle key
1) The
amount of energy released during a reaction tells nothing about the rate at
which that reaction will occur.
A) True
B) False
A. True
1) The
following methods are useful for cell homogenization:
A) Sonication
B) Freezing
and Thawing
C) Detergents
D) Enzymes
E) All
of the above
E. All of the above
1) Which
separates based on molecular weight?
A) Gel
filtration
B) Affinity
chromatography
C) Cation
exchange
D) Anion
exchange
E) Cation
or anion exchange
A. Gel Filtration
1) A
separation of a mixture of cations requires:
A) Another
cationic substance
B) An
anionic substance
C) An
electrically neutral, but slightly polar substance
D) An
electrically neutral, nonpolar substance
B. An anionic substance
1) The
following are all principles of electrophoresis, except:
A) Molecular
size
B) pI
C) Net
charge
D) Binding
to substrate
D. Binding to substrate
1) All
catalysts work by lowering the activation energy of the reaction.
A) True
B) False
A. True
1) When
the substrate concentration is low, the an enzyme reaction
A) Will
display zero order kinetics
B) Will
display first order kinetics
C) Will
display second order kinetics
D) Will
denature and cease to function
Will Display first order kinetics
1) A
lineweaver-burk plot is useful in the analysis of enzymatic reactions because
A) It
is easier to see if points deviate from a straight line, instead of a curve
B) It
allows you to calculate the exact values from a straight line
C) It
is an easy way to manipulate the data into a useful form
D) All
of the above
D. All of the above
1) The value of Vmax change in
A) Competitive
inhibition
B) Noncompetitive
inhibition
C) Both
forms
D) None
of the above
B. Non-competitive Inhibition
1) Generally speaking, a competitive inhibitor
and the substrate cannot both bind to the enzyme at the same time.
A) True
B) False
TRUE
1) The Michaelis-menton constant determines the
Vmax of an enzymatic reaction.
A) True
B) False
FALSE
1) What types of macromolecules are usually
separated on agarose gel electrophoresis gels?
Nucleic Acids (DNA)
Are
all enzymes proteins?
No but most are. There are some catalytic RNA's known.
1) What
are the elements of secondary structure in proteins? Pick one of these elements and outline in
detail the main characteristics of this form of secondary structure. Pay special attention to the forces involved,
and the arrangement of the structure.
Alpha Helix:
Stabilized by hydrogen bonds parallel to helix axis within backbone.
R Groups point out from Helix
B Sheet:
Hydrogen Bonds are perpendicular to axis of sheet
R Groups alternate above and below plane of sheet.
1) Explain in detail the significance of Km.
Km is a measure of affinity for substrate and enzyme.
Increase of Km = more dissociation and less affinity
Decrease of Km = less dissociation and more affinity
Using
a diagram of a basic tertiary structure, show three of the five forces that
stabilize this level of protein structure.
You MUST be specific, showing interacting atoms.
Look it up
Detail
the structural features of Secondary Structure in Proteins.
double
How
does the lock and key model of enzyme-substrate binding differ from the induced
fit model?
Lock and key model: substrate binds to
that portion of the enzyme with a complementary shape.
Induce fit model: Binding of the
substrate induces a change in the conformation of the enzyme that results in a
complementary fit.
Describe
in detail, how column chromatography work.
What components need to be present to run this sort of a
separation? Define all terms.
Column chromatography works to separate out
components of a mixture, through different interactions with a stationary
phase. The stationary phase is typically a polymer with linkers attached to it.
The stationary phase interacts with the components of the sampe and leads to separation.
The mobile phase contains the mixture, usually Ph a buffer and passes over the
