Lehninger Principles of Biochemistry Seventh Edition Solution Manual

Name: Lehninger Principles of Biochemistry Seventh Edition Solution Manual
Brand: Academic Documents Platform
Price: 15 USD
Availability: InStock
Author: Michael Davis

Lehninger Principles of Biochemistry Seventh Edition Solution Manual gives you access to textbook solutions that make learning easier and more efficient.

Michael Davis

Contributor

4.3

about 1 month ago

Preview (16 of 328)

The Absolute, Ultimate Guide to
Lehninger Principles of Biochemistry
Study Guide and Solutions Manual
Marcy Osgood
University of New Mexico School of Medicine
Karen Ocorr
Sanford Burnham Prebys Medical Discovery Institute
Solutions Manual based on
a previous edition by
Frederick Wedler
Robert Bernlohr
Ross Hardison
Teh-Hui Kao
Ming Tien
Pennsylvania State University
Seventh Edition

Preface vii
About the Authors ix
1 The Foundations of Biochemistry 1
Part I Structure and Catalysis
2 Water 11
3 Amino Acids, Peptides, and Proteins 21
4 The Three-Dimensional Structure
of Proteins 41
5 Protein Function 54
6 Enzymes 70
7 Carbohydrates and Glycobiology 87
8 Nucleotides and Nucleic Acids 100
9 DNA-Based Information Technologies 113
10 Lipids 123
11 Biological Membranes and Transport 134
12 Biosignaling 151
Part II Bioenergetics and
Metabolism
13 Bioenergetics and Biochemical Reaction
Types 172
14 Glycolysis, Gluconeogenesis, and the
Pentose Phosphate Pathway 183
15 Principles of Metabolic Regulation 195
16 The Citric Acid Cycle 206
17 Fatty Acid Catabolism 218
18 Amino Acid Oxidation and the Production
of Urea 228
19 Oxidative Phosphorylation 238
20 Photosynthesis and Carbohydrate
Synthesis in Plants 248
21 Lipid Biosynthesis 261
22 Biosynthesis of Amino Acids, Nucleotides,
and Related Molecules 274
23 Hormonal Regulation and Integration of
Mammalian Metabolism 286
Part III Information Pathways
24 Genes and Chromosomes 299
25 DNA Metabolism 307
26 RNA Metabolism 319
27 Protein Metabolism 331
28 Regulation of Gene Expression 343
v
Contents
Study Guide

1 The Foundations of Biochemistry S-1
Part I Structure and Catalysis
2 Water S-14
3 Amino Acids, Peptides, and Proteins S-29
4 The Three-Dimensional Structure of
Proteins S-44
5 Protein Function S-54
6 Enzymes S-63
7 Carbohydrates and Glycobiology S-78
8 Nucleotides and Nucleic Acids S-88
9 DNA-Based Information Technologies S-98
10 Lipids S-112
11 Biological Membranes and Transport S-120
12 Biosignaling S-132
Part II Bioenergetics and
Metabolism
13 Bioenergetics and Biochemical Reaction
Types S-141
14 Glycolysis, Gluconeogenesis, and the
Pentose Phosphate Pathway S-161
15 Principles of Metabolic Regulation S-174
16 The Citric Acid Cycle S-184
17 Fatty Acid Catabolism S-200
18 Amino Acid Oxidation and the Production
of Urea S-212
19 Oxidative Phosphorylation S-224
20 Photosynthesis and Carbohydrate
Synthesis in Plants S-236
21 Lipid Biosynthesis S-249
22 Biosynthesis of Amino Acids, Nucleotides,
and Related Molecules S-260
23 Hormonal Regulation and Integration of
Mammalian Metabolism S-268
Part III Information Pathways
24 Genes and Chromosomes S-276
25 DNA Metabolism S-285
26 RNA Metabolism S-297
27 Protein Metabolism S-304
28 Regulation of Gene Expression S-314
vi
Contents
Solutions Manual

vii
Preface
Learning a complex subject, such as biochemistry, is
very much like learning a foreign language.
In the study of a foreign language there are several
distinct components that must be mastered: the vo-
cabulary, the grammatical rules, and the integration of
these words and rules so they can be used to commu-
nicate ideas. Similarly, in the study of biochemistry
there is a very large (some would say vast) number of
new terms and concepts, as well as a complex set of
“rules” governing biochemical reactions that must all
be memorized. All of this information must be inte-
grated into an interrelated whole that describes bio-
logical systems.
Memorizing vocabulary and grammatical rules
will not make you fluent in a foreign language; nei-
ther will such memorization make you fluent in
biochemistry.
Similarly, listening to someone speak a foreign lan-
guage will not, by itself, make you more capable of
producing those same sounds, words, and sentences.
The key to mastery of any new subject area, whether
it is a foreign language or biochemistry, is the interac-
tion of memorization, practice, and application until
the information fits together into a coherent whole.
In this workbook we attempt to guide you through
the material presented in Lehninger Principles of
Biochemistry, Seventh Edition by Nelson and Cox.
The Step-by-Step Guide to each chapter includes
three parts:
• A one- to two-page summary of the Major Concepts
helps you to see the “big picture” for each chapter.
• What to Review helps you make direct connections
between the current material and related informa-
tion presented elsewhere in the text.
• Topics for Discussion for each section and subsec-
tion in the chapter focus your attention on the main
points being presented and help you internalize the
information by using it.
• Discussion Questions for Study Groups are
questions that are especially suited to Study Groups,
either because they pull together several points
made in the chapter or because they are more in-
volved questions that would benefit from collabora-
tive insight.
Each chapter also includes a Self-Test for you to
assess your progress in mastering biochemical ter-
minology and facts, and learning to integrate and
apply that information.
• Do You Know the Terms? asks you to complete a
crossword puzzle using the new vocabulary intro-
duced in the chapter.
• Do You Know the Facts? tests how well you have
learned the “rules” of biochemistry.
• Applying What You Know tests how well you
“speak the language” of biochemistry, often in an
experimental or metabolically relevant context.
Two especially popular features of the Absolute, Ulti-
mate Guide are:
• The Biochemistry Online problems will expose you
to just a few of the analytical resources that are
available to scientists on the Internet. The molecu-
lar models are fun to play with, and many of the
questions provide you with an opportunity to
analyze “data” as you might in an actual laboratory
setting.
• The Cell Map is based on many semesters of use by
our students. It is designed to help you place the
biochemical pathways that you are learning about
into their proper cellular perspective. The Cell Map
questions tell you what to include in your Map, but
you can be creative!
Students have told us it is a great study aid, that
really helped them to make the connections between
the various pathways.

In our experience, this material can best be assimi-
lated when it is discussed in a study group.
A study group is nothing more than two to four people
who get together on a regular basis (weekly) to “speak
biochemistry.” This type of interaction is critical to flu-
ency in a foreign language and is no less critical in the
successful assimilation of biochemistry. We designed
our Step-by-Step Guide to each chapter with study
groups in mind. The questions posed for each section
can be used as springboards for study group discus-
sions. We purposefully have not supplied answers to
this section to force you to wrestle with the concepts.
It is the struggle that will make you learn the material.
In addition, because most of the answers can be read-
ily worked out by a careful reading of the section of
the text, the questions will focus your attention on the
more important aspects of the material.
Detailed Solutions to all the end-of-chapter textbook
problems are included as a separate section in the
Absolute, Ultimate Guide.
We have taken great care to ensure that the solutions
are correct, complete, and informative. The final
answer to numerical problems has been rounded
off to reflect the number of significant figures in
the data.
We thank each and every one of our students for their
invaluable feedback and input, which have helped to
make this study guide its absolute and ultimate best.
viii Preface

Loading page 6...

About the Authors
ix
Karen Ocorr received her Ph.D. from Wesleyan University, where she studied the physiology
and neurochemistry of the lobster cardiac ganglion. As an NIH postdoctoral research fellow
at the University of Texas, she examined the roles of enzymes and second messengers
in neuronal plasticity in Aplysia californica. She continued these investigations at the
California Institute of Technology and Stanford University, examining the role of intracellular
signaling underlying long-term potentiation in the vertebrate hippocampus. She taught
Introductory Biochemistry for 10 years at the University of Michigan, Ann Arbor, where she
also taught Animal Physiology, Cell Biology, and Introductory Biology for Non-Majors. She
also taught Introductory Biochemistry for four years as a visiting Professor at the Hunan
Normal University in Changsha, China. Currently she is an Assistant Professor at SBP
Medical Discovery Institute in La Jolla, California, where she is researching the roles of ion
channels in cardiomyopathies. She currently teaches graduate and medical students at both
the SBP Medical Discovery Institute and the University of California–San Diego.
Marcy Osgood received her Ph.D. from Rensselaer Polytechnic Institute. After two
postdoctoral positions, she became an Assistant Professor in the Department of Physical
Sciences at Albany College of Pharmacy, Union University. She was then a Lecturer in the
Biology Department at the University of Michigan, Ann Arbor for nine years, where her
research interests began to focus on educational issues. Her current position is as Associate
Professor in the Department of Biochemistry and Molecular Biology and Assistant Dean of
Undergraduate Medical Education at the University of New Mexico School of Medicine. Her
current research efforts deal with assessment of problem-solving strategies.
Osgood and Ocorr have collaborated for 10 years to develop effective techniques for teaching
biochemistry, all of which are based on educational research. This study guide is the result of
these efforts and embodies much of what they have found to be effective over years of
instruction at many levels and in many areas of the biological sciences. It includes thousands
of discussion, quiz, and exam questions from their biochemistry courses. Osgood and Ocorr
have been responsible for teaching biochemistry to more than 10,000 undergraduate
students.

Loading page 7...

The Foundations
of Biochemistry
chapter
1
S-1
1. The Size of Cells and Their Components
(a) If you were to magnify a cell 10,000-fold (typical of the magnification achieved using an electron
microscope), how big would it appear? Assume you are viewing a “typical” eukaryotic cell with a
cellular diameter of 50 mm.
(b) If this cell were a muscle cell (myocyte), how many molecules of actin could it hold? Assume
the cell is spherical and no other cellular components are present; actin molecules are spherical,
with a diameter of 3.6 nm. (The volume of a sphere is 4/3 pr3
.)
(c) If this were a liver cell (hepatocyte) of the same dimensions, how many mitochondria could it
hold? Assume the cell is spherical; no other cellular components are present; and the
mitochondria are spherical, with a diameter of 1.5 mm.
(d) Glucose is the major energy-yielding nutrient for most cells. Assuming a cellular concentration of
1 mM (i.e., 1 millimole/L), calculate how many molecules of glucose would be present in our
hypothetical (and spherical) eukaryotic cell. (Avogadro’s number, the number of molecules in 1
mol of a nonionized substance, is 6.02 10 23 .)
(e) Hexokinase is an important enzyme in the metabolism of glucose. If the concentration of hexokinase
in our eukaryotic cell is 20 mM, how many glucose molecules are present per hexokinase molecule?
Answer
(a) The magnified cell would have a diameter of 50 10 4 mm 500 10 3 mm 500 mm,
or 20 inches—about the diameter of a large pizza.
(b) The radius of a globular actin molecule is 3.6 nm/2 1.8 nm; the volume of the
molecule, in cubic meters, is (4/3)(3.14)(1.8 109 m)3 2.4 1026 m3
.*
The number of actin molecules that could fit inside the cell is found by dividing the cell
volume (radius 25 mm) by the actin molecule volume. Cell volume (4/3)(3.14)(25
106 m)3 6.5 1014 m3
. Thus, the number of actin molecules in the hypothetical
muscle cell is
(6.5 1014 m3
)/(2.4 1026 m3
) 2.7 10 12 molecules
or 2.7 trillion actin molecules.
*Significant figures: In multiplication and division, the answer can be expressed with no
more significant figures than the least precise value in the calculation. Because some of the
data in these problems are derived from measured values, we must round off the calculated
answer to reflect this. In this first example, the radius of the actin (1.8 nm) has two significant
figures, so the answer (volume of actin

Loading page 8...

Loading page 9...

Loading page 10...

5. Fast Axonal Transport Neurons have long thin processes called axons, structures specialized for
conducting signals throughout the organism’s nervous system. Some axonal processes can be as long
as 2 m—for example, the axons that originate in your spinal cord and terminate in the muscles of your
toes. Small membrane-enclosed vesicles carrying materials essential to axonal function move along mi-
crotubules of the cytoskeleton, from the cell body to the tips of the axons. If the average velocity of a
vesicle is 1 mm/s, how long does it take a vesicle to move from a cell body in the spinal cord to the
axonal tip in the toes?
Answer Transport time equals distance traveled/velocity, or
(2 10 6 mm)/(1 mm/s) 2 10 6 s
or about 23 days!
6. Is Synthetic Vitamin C as Good as the Natural Vitamin? A claim put forth by some purveyors of
health foods is that vitamins obtained from natural sources are more healthful than those obtained by
chemical synthesis. For example, pure L-ascorbic acid (vitamin C) extracted from rose hips is better
than pure L-ascorbic acid manufactured in a chemical plant. Are the vitamins from the two sources dif-
ferent? Can the body distinguish a vitamin’s source?
Answer The properties of the vitamin—like any other compound—are determined by its
chemical structure. Because vitamin molecules from the two sources are structurally identical,
their properties are identical, and no organism can distinguish between them. If different vitamin
preparations contain different impurities, the biological effects of the mixtures may vary with
the source. The ascorbic acid in such preparations, however, is identical.
7. Identification of Functional Groups Figures 1–16 and 1–17 show some common functional groups
of biomolecules. Because the properties and biological activities of biomolecules are largely deter-
mined by their functional groups, it is important to be able to identify them. In each of the compounds
below, circle and identify by name each functional group.
S-4 Chapter 1 The Foundations of Biochemistry
H
H
Ethanolamine
(a)
C
H
H
C OHH 3 N
Glycerol
(b)
H
H
C OH
H C OH
H C OH
H
Threonine, an
amino acid
(d)
H
CH3
C OH
C H
Pantothenate,
a vitamin
(e)
H3 C
CH2 OH
C CH3
H C OH
C O
NH
Phosphoenolpyruvate,
an intermediate in
glucose metabolism
(c)
C C
O
HO P
O
H
H
CH2
CH2
C
O
D-Glucosamine
(f )
H
CH 2OH
C OH

Loading page 11...

Answer
(a) ONH 3
amino; OOH hydroxyl
(b) OOH hydroxyl (three)
(c) OP(OH)O 2
phosphoryl (in its ionized form); OCOO carboxyl
(d) OCOO carboxyl; ONH 3
amino; OOH hydroxyl; OCH 3 methyl (two)
(e) OCOO carboxyl; OCOONHO amide; OOH hydroxyl (two); OCH 3 methyl
(two)
(f) OCHO aldehyde; ONH 3
amino; OOH hydroxyl (four)
8. Drug Activity and Stereochemistry The quantitative differences in biological activity between the
two enantiomers of a compound are sometimes quite large. For example, the D isomer of the drug iso-
proterenol, used to treat mild asthma, is 50 to 80 times more effective as a bronchodilator than the
L isomer. Identify the chiral center in isoproterenol. Why do the two enantiomers have such radically
different bioactivity?
Answer A chiral center, or chiral carbon, is a carbon atom that is bonded to four different
groups. A molecule with a single chiral center has two enantiomers, designated D and L (or in the
RS system, S and R). In isoproterenol, only one carbon (asterisk) has four different groups
around it; this is the chiral center:
The bioactivity of a drug is the result of interaction with a biological “receptor,” a protein
molecule with a binding site that is also chiral and stereospecific. The interaction of the D isomer
of a drug with a chiral receptor site will differ from the interaction of the L isomer with that site.
9. Separating Biomolecules In studying a particular biomolecule (a protein, nucleic acid, carbohy-
drate, or lipid) in the laboratory, the biochemist first needs to separate it from other biomolecules in
the sample—that is, to purify

Loading page 12...

10. Silicon-Based Life? Silicon is in the same group of the periodic table as carbon and, like carbon, can
form up to four single bonds. Many science fiction stories have been based on the premise of silicon-
based life. Is this realistic? What characteristics of silicon make it less well adapted than carbon as the
central organizing element for life? To answer this question, consider what you have learned about car-
bon’s bonding versatility, and refer to a beginning inorganic chemistry textbook for silicon’s bonding
properties.
Answer It is improbable that silicon could serve as the central organizing element for life under
such conditions as those found on Earth for several reasons. Long chains of silicon atoms are not
readily synthesized, and thus the polymeric macromolecules necessary for more complex func-
tions would not readily form. Also, oxygen disrupts bonds between two silicon atoms, so silicon-
based life-forms would be unstable in an oxygen-containing atmosphere. Once formed, the bonds
between silicon and oxygen are extremely stable and difficult to break, which would prevent the
breaking and making (degradation and synthesis) of biomolecules that is essential to the
processes of living organisms.
11. Drug Action and Shape of Molecules Some years ago two drug companies marketed a drug under
the trade names Dexedrine and Benzedrine. The structure of the drug is shown below.
The physical properties (C, H, and N analysis, melting point, solubility, etc.) of Dexedrine and
Benzedrine were identical. The recommended oral dosage of Dexedrine (which is still available)
was 5 mg/day, but the recommended dosage of Benzedrine (no longer available) was twice that.
Apparently, it required considerably more Benzedrine than Dexedrine to yield the same physiologi-
cal response. Explain this apparent contradiction.
Answer Only one of the two enantiomers of the drug molecule (which has a chiral center) is
physiologically active, for reasons described in the answer to Problem 3 (interaction with a
stereospecific receptor site). Dexedrine, as manufactured, consists of the single enantiomer
( D -amphetamine) recognized by the receptor site. Benzedrine was a racemic mixture (equal
amounts of D and L isomers), so a much larger dose was required to obtain the same effect.
12. Components of Complex Biomolecules Figure 1–11 shows the major components of complex bio-
molecules. For each of the three important biomolecules below (shown in their ionized forms at physi-
ological pH), identify the constituents.
(a) Guanosine triphosphate (GTP), an energy-rich nucleotide that serves as a precursor to RNA:
S-6 Chapter 1 The Foundations of Biochemistry
CCH2 CH3
NH2
H
N
C
O
O
O
OP OP O N
N NH
NH2
OP CH 2
O
O
O
O
H H
H H
OH OH
O

Loading page 13...

Loading page 14...

Loading page 15...

Answer Determining the chirality of an asymmetric carbon requires ranking the four sub-
stituents in order of decreasing atomic number or decreasing molecular weight with immediate
attachments. The asymmetric carbon is propranolol in the question because it is shown with a
black triangular wedge bond to the hydroxyl. This means that the bond is in front of the plane
of the page.
The four substituents of the alcohol carbon would be ranked (1) the hydroxyl, (2) C—O,
(3) C—N, and (4) a hydrogen (not shown), which is behind the plane of the page. With this
lowest-priority “group” pointing away, the other groups in decreasing priority (1 to 3) are in the
sequence down, left, right—clockwise—so the configuration is (R).
15. Naming Stereoisomers with Two Chiral Carbons Using the RS System The (R,R) isomer of
methylphenidate (Ritalin) is used to treat attention deficit hyperactivity disorder (ADHD). The (S,S)
isomer is an antidepressant. Identify the two chiral carbons in the structure below. Is this the (R,R) or
the (S,S) isomer? Draw the other isomer.
Chapter 1 The Foundations of Biochemistry S-9
O
OH
N
H
O
O
H
HN
O
O
H
NH
Answer The asymmetric carbons can be identified by the presence of the wedge-shaped bonds
indicating the spatial relationship of the bound groups. Wedge bonds always have the narrow
end at the chiral carbon and the wide end at the attached atom or group. Solid wedge bonds
project toward the reader; dashed wedge bonds project away from the reader, behind the plane
of the paper. In this molecule, one wedge bond is solid black; the benzene ring at the wide end
is coming out of the plane of the paper toward the reader. The hydrogen at the wide end of the
dashed wedge bond projects behind the paper.
The chiral center on the ring has the lowest priority group, the hydrogen atom, projecting
away, so we can evaluate it as it stands. The remaining attached atoms, in priority order, are
(1) nitrogen, (2) the carbon with two carbons attached to it, and (3) the ring carbon with one
carbon attached. In decreasing priority (1 to 3) the sequence is left, down, right—counterclock-
wise—so the configuration is (S). The second chiral center also has the lowest priority group,
the hydrogen atom, projecting away from the reader. The priority order of the other sub-
stituents is (1) the carboxyl group (with two oxygens attached), (2) the nitrogen ring, and (3)
the benzene ring. In decreasing priority (1 to 3) the sequence is right, left, down—counter-
clockwise—so the configuration around the second chiral center is also (S). This is the (S,S)
configuration of methylphenidate.
To draw the (R,R) configuration, given the (S,S) configuration, make a complete mirror
image.
To maintain the original orientation of the molecule, it is often possible to begin by making the
dashed wedge bonds solid and the solid wedge bonds dashed. However, it is essential to verify
the configuration and make adjustments as needed, because this method is not foolproof.

Loading page 16...

15 more pages available. Scroll down to load them.

Preview Mode

100%

Study Now!

XY-Copilot AI

Unlimited Access

Secure Payment

Instant Access

24/7 Support

Document Chat

Document Details

Subject

Biochemistry

Lehninger Principles of Biochemistry Seventh Edition Solution Manual

Study Now!

Document Details

Related Documents

Lehninger Principles of Biochemistry Sixth Edition Solution Manual

Lehninger Principles of Biochemistry Seventh Edition Test Bank

Kami Export Biological Molecules POGIL

Macromolecules Building Blocks of Life for Elephan

Investigating the Effect of pH on Peroxidase Activity and Its Implications for Industrial Applications

Investigating The Effect Of Hydrogen Peroxide On Enzymatic Activity In Various Eatable Substrates

Solution Manual For Experiments in Biochemistry: A Hands-on Approach, 2nd Edition

Solution Manual For Essential Biochemistry, 4th Edition

Solution Manual For Essentials of General, Organic, and Biochemistry, 3rd Edition

Solution Manual For Laboratory Experiments for Introduction to General, Organic and Biochemistry, 8th Edition

Company

Explore

Study Tools