100% satisfaction guarantee Immediately available after payment Both online and in PDF No strings attached 4.6 TrustPilot
logo-home
Exam (elaborations)

Fundamentals of Biochemistry Life at the Molecular Level 5th Edition 2025 Brand NEW

Rating
-
Sold
-
Pages
25
Grade
A+
Uploaded on
06-04-2025
Written in
2024/2025

Fundamentals of Biochemistry Life at the Molecular Level 5th Edition 2025 Brand NEW

Institution
Fundamentals Of Biochemistry Life At The Molecular
Course
Fundamentals of Biochemistry Life at the Molecular










Whoops! We can’t load your doc right now. Try again or contact support.

Written for

Institution
Fundamentals of Biochemistry Life at the Molecular
Course
Fundamentals of Biochemistry Life at the Molecular

Document information

Uploaded on
April 6, 2025
Number of pages
25
Written in
2024/2025
Type
Exam (elaborations)
Contains
Questions & answers

Subjects

Content preview

Fundamentals of Biochemistry Life at
the Molecular Level 5th Edition 2025
Brand NEW
____________________________________________________________________________________

A compound has a pKa of 7.4. To 100 mL of a 1.0 M solution of this compound at pH 8.0 is added 30
mL of 1.0 M hydrochloric acid. The resulting solution is pH:

A) 6.5
B) 6.8
C) 7.2
D) 7.4
E) 7.5

 7.4

the henderson hasselbach equation

 relates the pH of a solution to the pKa and the concentrations of acid and conjugate base.

Consider an acetate buffer, initially at the same pH as its pKa (4.76). When sodium hydroxide (NaOH)
is mixed with this buffer, the:

A) pH remains constant.
B) pH rises more than if an equal amount of NaOH is added to an acetate buffer initially at pH 6.76.
C) pH rises more than if an equal amount of NaOH is added to unbuffered water at pH 4.76.
D) ratio of acetic acid to sodium acetate in the buffer falls.
E) sodium acetate formed precipitates because it is less soluble than acetic acid.

 ratio of acetic acid to sodium acetate in the buffer falls

a compound is known to have a free amino group with pka of 8.8, and one other ionizable groups with
a pka between 5 and 7. to 100 mL of a 0.2 M solution of this compound at pH 8.2 was added to a 40
ML solution of 0.2 M Hcl. the pkas of the second ionizable group is

 5.6

the buffers are made by combining a 1 M solution of acetic acid with a 1M solution of sodium acetate
in the ratios below: which of these statements is true of the resulting buffers

 ph of buffer 1 > ph of buffer 2 > ph of buffer 3

A 1.0 M solution of a compound with 2 ionizable groups (pKa's = 6.2 and 9.5; 100 mL total) has a pH of
6.8. If a biochemist adds 60 mL of 1.0 M HCl to this solution, the solution will change to pH:

,A) 5.60
B) 8.90
C) 9.13
D) 9.32
E) The pH cannot be determined from this information.

 5.60

in which reaction does water not participate as a reactant

 production of gaseous carbon dioxide from bicarbonate

which of the following properties of water does not contribute to the fitness of the aqueous
environment for living organisms

 the very low molecular weight of water

One of the enzymes involved in glycolysis, aldolase, requires Zn2+ for catalysis. Under conditions of
zinc deficiency, when the enzyme may lack zinc, it would be referred to as the:

A) apoenzyme.
B) coenzyme.
C) holoenzyme.
D) prosthetic group.
E) substrate.

 apoenzyme

which one of the following is not among the six internationally accepted classes of enzymes

 polymerases

Enzymes are potent catalysts because they:

A) are consumed in the reactions they catalyze.
B) are very specific and can prevent the conversion of products back to substrates.
C) drive reactions to completion while other catalysts drive reactions to equilibrium.
D) increase the equilibrium constants for the reactions they catalyze.
E) lower the activation energy for the reactions they catalyze.

 lower the activation energy for the reactions they catalyze

The role of an enzyme in an enzyme-catalyzed reaction is to:

A) bind a transition state intermediate, such that it cannot be converted back to substrate.
B) ensure that all of the substrate is converted to product.
C) ensure that the product is more stable than the substrate.
D) increase the rate at which substrate is converted into product.
E) make the free-energy change for the reaction more favorable.

,  increase the rate at which substrate is converted into product

which one of the following statements is true of enzyme catalysts

 They can increase the reaction rate for a given reaction by a thousand-fold or more.

which one of the following statements is true of enzyme catalysts

 They lower the activation energy for the conversion of substrate to product.

Which of the following statements is false?

 For S --> P, a catalyst shifts the reaction equilibrium to the right.

Enzymes differ from other catalysts in that only enzymes:

A) are not consumed in the reaction.
B) display specificity toward a single reactant.
C) fail to influence the equilibrium point of the reaction.
D) form an activated complex with the reactants.
E) lower the activation energy of the reaction catalyzed.

 display specificity toward a single reactant.

the benefit of measuring the initial rate of a reaction Vo is that at the beginning of a reaction

 changes in [S] are negligible, so [S] can be treated as a constant.

which of the following statements about a plot of Vo vs. [S] for an enzyme that follows michaelis-
mention kinetics is false

 at very high [S], the velocity curve becomes a horizontal like that intersects the Y-axis at Km

Using this reaction, the rate of breakdown of the enzyme-substrate complex can be described by the
expression:

 k-1 [ES] + k2 [ES].

The steady state assumption, as applied to enzyme kinetics, implies:

A) Km = Ks.
B) the enzyme is regulated.
C) the ES complex is formed and broken down at equivalent rates.
D) the Km is equivalent to the cellular substrate concentration.
E) the maximum velocity occurs when the enzyme is saturated.

 the ES complex is formed and broken down at equivalent rates.

the most abundant molecule in the human body

 H2O

during chemical evolution, small organic molecules condense to form more complex molecules called
$16.69
Get access to the full document:

100% satisfaction guarantee
Immediately available after payment
Both online and in PDF
No strings attached

Get to know the seller
Seller avatar
ryanemmerson

Get to know the seller

Seller avatar
ryanemmerson Chamberlain School Of Nursing
View profile
Follow You need to be logged in order to follow users or courses
Sold
1
Member since
11 months
Number of followers
0
Documents
154
Last sold
9 months ago

0.0

0 reviews

5
0
4
0
3
0
2
0
1
0

Why students choose Stuvia

Created by fellow students, verified by reviews

Quality you can trust: written by students who passed their tests and reviewed by others who've used these notes.

Didn't get what you expected? Choose another document

No worries! You can instantly pick a different document that better fits what you're looking for.

Pay as you like, start learning right away

No subscription, no commitments. Pay the way you're used to via credit card and download your PDF document instantly.

Student with book image

“Bought, downloaded, and aced it. It really can be that simple.”

Alisha Student

Frequently asked questions