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Essential Biochemistry [Loose-leaf]

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  • Formāts: Loose-leaf, 744 pages, height x width x depth: 272x214x24 mm, weight: 1361 g, Contains 1 Loose-leaf
  • Izdošanas datums: 26-May-2015
  • Izdevniecība: John Wiley & Sons Inc
  • ISBN-10: 1118441680
  • ISBN-13: 9781118441688
Citas grāmatas par šo tēmu:
  • Formāts: Loose-leaf, 744 pages, height x width x depth: 272x214x24 mm, weight: 1361 g, Contains 1 Loose-leaf
  • Izdošanas datums: 26-May-2015
  • Izdevniecība: John Wiley & Sons Inc
  • ISBN-10: 1118441680
  • ISBN-13: 9781118441688
Citas grāmatas par šo tēmu:
This text is an unbound, binder-ready edition.

This book is comprised of biology, pre-med, and allied health topics and presents a broad, but not overwhelming base of biochemical coverage that focuses on the chemistry behind the biology. Furthermore, it relates the chemical concepts that scaffold the biology of biochemistry, providing practical knowledge as well as many problem-solving opportunities to hone skills. Key Concepts and Concept Review features help students to identify and review important takeaways in each section.
part one Foundations
1 The Chemical Basis Of Life
1(23)
1-1 What is Biochemistry?
2(1)
1-2 Biological Molecules
3(7)
Cells contain four major types of biomolecules
5(1)
There are three major kinds of biological polymers
6(4)
1-3 Energy and Metabolism
10(4)
Enthalpy and entropy are components of free energy
10(1)
Δ G is less than zero for a spontaneous process
11(1)
Life is thermodynamically possible
12(2)
1-4 The Origin and Evolution of Life
14(10)
The prebiotic world
14(2)
Origins of modern cells
16
Box 1-A Biochemistry Note Units Used in Biochemistry
7(10)
Box 1-B Biochemistry Note How Does Evolution Work?
17(2)
Bioinformatics Project 1 The Biochemical Literature
19(5)
2 Aqueous Chemistry
24(27)
2-1 Water Molecules form Hydrogen Bonds
25(5)
Hydrogen bonds are one type of electrostatic force
26(3)
Water dissolves many compounds
29(1)
2-2 The Hydrophobic Effect
30(3)
Amphiphilic molecules experience both hydrophilic interactions and the hydrophobic effect
31(1)
The hydrophobic core of a lipid bilayer is a barrier to diffusion
32(1)
2-3 Acid-Base Chemistry
33(8)
[ H+] and [ OH-] are inversely related
34(2)
The pH of a solution can be altered
36(1)
A pK value describes an acid's tendency to ionize
37(1)
The pH of a solution of acid is related to the pK
37(4)
2-4 Tools and Techniques: Buffers
41(10)
Box 2-A Biochemistry Note Why Do Some Drugs Contain Fluorine?
28(5)
Box 2-B Biochemistry Note sweat, exercise, and sports Drinks
33(2)
Box 2-C Biochemistry Note Atmospheric CO2 and Ocean Acidification
35(8)
Box 2-D Clinical Connection Acid-Base Balance in Humans
43(8)
part two Molecular Structure And Function
3 From Genes To Proteins
51(36)
3-1 DNA Is the Genetic Material
52(9)
Nucleic acids are polymers of nucleotides
53(1)
Some nucleotides have other functions
54(2)
DNA is a double helix
56(3)
RNA is single-stranded
59(1)
DNA can be denatured and renatured
59(2)
3-2 Genes Encode Proteins
61(4)
A mutated gene can cause disease
63(2)
3-3 Genomics
65(5)
Gene number is roughly correlated with organismal complexity
65(2)
Genes are identified by comparing sequences
67(1)
Genomic data can be linked to disease
68(2)
3-4 Tools and Techniques: Manipulating DNA
70(17)
DNA sequencing uses DNA polymerase to make a complementary strand
70(2)
The polymerase chain reaction amplifies DNA
72(3)
Restriction enzymes cut DNA at specific sequences
75(1)
DNA fragments are joined to produce recombinant DNA
76(1)
Cloned genes yield valuable products
77(2)
Genetically modified organisms have practical applications
79(1)
Gene therapy can cure some human diseases
79
Box 3-A Clinical Connection Discovery of the Cystic Fibrosis Gene
64(10)
Box 3-B Biochemistry Note DNA Fingerprinting
74(7)
Bioinformatics Project 2 Databases for the Storage and "Mining" of Genome Sequences
81(6)
4 Protein Structure
87(34)
4-1 Proteins Are Chains of Amino Acids
89(7)
The 20 amino acids have different chemical properties
89(2)
Peptide bonds link amino acids in proteins
91(4)
The amino acid sequence is the first level of protein structure
95(1)
4-2 Secondary Structure: The Conformation of the Peptide Group
96(3)
The a helix exhibits a twisted backbone conformation
97(1)
The β sheet contains multiple polypeptide strands
97(1)
Proteins also contain irregular secondary structure
98(1)
4-3 Tertiary Structure and Protein Stability
99(8)
Proteins have hydrophobic cores
100(2)
Protein structures are stabilized mainly by the hydrophobic effect
102(1)
Cross-links help stabilize proteins
102(2)
Protein folding begins with the formation of secondary structures
104(3)
4-4 Quaternary Structure
107(1)
4-5 Tools and Techniques: Analyzing Protein Structure
108(13)
Chromatography takes advantage of a polypeptide's unique properties
108(3)
Mass spectrometry reveals amino acid sequences
111(2)
Protein structures are determined by X-ray crystallography, electron crystallography, and NMR spectroscopy
113
Box 4-A Biochemistry Note Does Chirality Matter?
89(3)
Box 4-B Biochemistry Note Monosodium Glutamate
92(13)
Box 4-C Clinical Connection Protein Misfolding and Disease
105(8)
Box 4-D Biochemistry Note Mass Spectrometry Applications
113(2)
Bioinformatics Project 3 Visualizing Three-Dimensional Protein Structures
115(6)
5 Protein Function
121(37)
5-1 Myoglobin and Hemoglobin: Oxygen-Binding Proteins
122(11)
Oxygen binding to myoglobin depends on the oxygen concentration
123(1)
Myoglobin and hemoglobin are related by evolution
124(2)
Oxygen binds cooperatively to hemoglobin
126(2)
A conformational shift explains hemoglobin's cooperative behavior
128(1)
H+ ions and bisphosphoglycerate regulate oxygen binding to hemoglobin in vivo
129(4)
5-2 Structural Proteins
133(11)
Microfilaments are made of actin
133(1)
Actin filaments continuously extend and retract
134(2)
Tubulin forms hollow microtubules
136(1)
Some drugs affect microtubules
137(1)
Keratin is an intermediate filament
138(2)
Collagen is a triple helix
140(2)
Collagen molecules are covalently cross-linked
142(2)
5-3 Motor Proteins
144(14)
Myosin has two heads and a long tail
144(2)
Myosin operates through a lever mechanism
146(1)
Kinesin is a microtubule-associated motor protein
146(4)
Kinesin is a processive motor
150
Box 5-A Biochemistry Note Erythropoietin Boosts Red Blood Cell Production
126(1)
Box 5-B Biochemistry Note Carbon Monoxide Poisoning
127(3)
Box 5-C Clinical Connection Hemoglobin Mutations
130(11)
Box 5-D Biochemistry Note Vitamin C Deficiency Causes Scurvy
141(2)
Box 5-E Clinical Connection Genetic Collagen Diseases
143(4)
Box 5-F Biochemistry Note Myosin Mutations and Deafness
147(4)
Bioinformatics Project 4 Using Databases to Compare and Identify Related Protein Sequences
151(7)
6 How Enzymes Work
158(30)
6-1 What Is an Enzyme?
159(3)
Enzymes are usually named after the reaction they catalyze
161(1)
6-2 The Chemistry of Catalysis
162(9)
A catalyst provides a reaction pathway with a lower activation energy barrier
164(1)
Enzymes use chemical catalytic mechanisms
164(5)
The catalytic triad of chymotrypsin promotes peptide bond hydrolysis
169(2)
6-3 The Unique Properties of Enzyme Catalysts
171(3)
Enzymes stabilize the transition state
171(2)
Efficient catalysis depends on proximity and orientation effects
173(1)
The active site microenvironment promotes catalysis
173(1)
6-4 Some Additional Features of Enzymes
174(14)
Not all serine proteases are related by evolution
174(1)
Enzymes with similar mechanisms exhibit different substrate specificity
175(1)
Chymotrypsin is activated by proteolysis
176(3)
Protease inhibitors limit protease activity
179
Box 6-A Biochemistry Note Depicting Reaction Mechanisms
167(10)
Box 6-B Clinical Connection Blood Coagulation Requires a Cascade of Proteases
177(11)
7 Enzyme Kinetics And Inhibition
188(32)
7-1 Introduction to Enzyme Kinetics
189(2)
7-2 Derivation and Meaning of the Michaelis-Menten Equation
191(9)
Rate equations describe chemical processes
191(1)
The Michaelis-Menten equation is a rate equation for an enzyme-catalyzed reaction
192(3)
Km is the substrate concentration at which velocity is half-maximal
195(1)
The catalytic constant describes how quickly an enzyme can act
195(1)
kcat/KM indicates catalytic efficiency
195(1)
KM and Vmax are experimentally determined
196(2)
Not all enzymes fit the simple Michaelis-Menten model
198(2)
7-3 Enzyme Inhibition
200(20)
Some inhibitors act irreversibly
202(1)
Competitive inhibition is the most common form of reversible enzyme inhibition
203(2)
Transition state analogs inhibit enzymes
205(2)
Other types of inhibitors affect Vmax
207(2)
Allosteric enzyme regulation includes inhibition and activation
209(2)
Several factors may influence enzyme activity
211
Box 7-A Clinical Connection Drug Development
200(6)
Box 7-B Biochemistry Note Inhibitors of HIV Protease
206(6)
Bioinformatics Project 5 Enzyme Inhibitors and Rational Drug Design
212(8)
8 Lipids And Membranes
220(21)
8-1 Lipids
221(6)
Fatty acids contain long hydrocarbon chains
221(2)
Some lipids contain polar head groups
223(2)
Lipids perform a variety of physiological I functions
225(2)
8-2 The Lipid Bilayer
227(3)
The bilayer is a fluid structure
227(3)
Natural bilayers are asymmetric
230(1)
8-3 Membrane Proteins
230(3)
Integral membrane proteins span the bilayer
231(1)
An a helix can cross the bilayer
231(1)
A transmembrane β sheet forms a barrel
232(1)
Lipid-linked proteins are anchored in the membrane
232(1)
8-4 The Fluid Mosaic Model
233(8)
Membrane glycoproteins face the cell exterior
234
Box 8-A Biochemistry Note Omega-3 Fatty Acids
222(3)
Box 8-B Clinical Connection The Lipid Vitamins A, D, E, and K
225(16)
9 Membrane Transport
241(25)
9-1 The Thermodynamics of Membrane Transport
242(4)
Ion movements alter membrane potential
243(2)
Transporters mediate transmembrane ion movement
245(1)
9-2 Passive Transport
246(6)
Porins are β barrel proteins
246(1)
Ion channels are highly selective
247(1)
Gated channels undergo conformational changes
248(2)
Aquaporins are water-specific pores
250(1)
Some transport proteins alternate between conformations
251(1)
9-3 Active Transport
252(3)
The Na, K-ATPase changes conformation as it pumps ions across the membrane
252(1)
ABC transporters mediate drug resistance
253(1)
Secondary active transport exploits existing gradients
254(1)
9-4 Membrane Fusion
255(11)
SNAREs link vesicle and plasma membranes
256(3)
Membrane fusion requires changes in bilayer curvature
259
Box 9-A Biochemistry Note Pores Can Kill
248(9)
Box 9-B Biochemistry Note Some Drugs Interfere with Neuronal Signaling
257(1)
Box 9-C Clinical Connection Antidepressants Block Serotonin Transport
258(8)
10 Signaling
266(24)
10-1 General Features of Signaling Pathways
267(4)
A ligand binds to a receptor with a characteristic affinity
267(2)
Most signaling occurs through two types of receptors
269(1)
The effects of signaling are limited
270(1)
10-2 G Protein Signaling Pathways
271(6)
G protein--coupled receptors include seven transmembrane helices
271(1)
The receptor activates a G protein
272(1)
Adenylate cyclase generates the second messenger cyclic AMP
273(1)
Cyclic AMP activates protein kinase A
273(2)
Signaling pathways are also switched off
275(1)
The phosphoinositide signaling pathway generates two second messengers
276(1)
Calmodulin mediates some Ca2+ signals
277(1)
10-3 Receptor Tyrosine Kinases
277(4)
The insulin receptor has two ligand-binding sites
277(1)
The receptor undergoes autophosphorylation
278(3)
10-4 Lipid Hormone Signaling
281(9)
Eicosanoids are short-range signals
282
Box 10-A Biochemistry Note Bacterial Quorum Sensing
268(12)
Box 10-B Biochemistry Note Cell Signaling and Cancer
280(2)
Box 10-C Biochemistry Note Oral Contraceptives
282(1)
Box 10-D Biochemistry Note Aspirin and Other Inhibitors of Cyclooxygenase
283(7)
11 Carbohydrates
290(18)
11-1 Monosaccharides
291(3)
Most carbohydrates are chiral compounds
291(1)
Cyclization generates α and β anomers
292(1)
Monosaccharides can be derivatized in many different ways
293(1)
11-2 Polysaccharides
294(5)
Lactose and sucrose are the most common disaccharides
295(1)
Starch and glycogen are fuel storage molecules
296(1)
Cellulose and chitin provide structural support
296(2)
Bacterial polysaccharides form a biofilm
298(1)
11-3 Glycoproteins
299(9)
N-linked oligosaccharides undergo processing
299(1)
O-linked oligosaccharides tend to be large
300(1)
What is the purpose of the oligosaccharide groups?
300(1)
Proteoglycans contain long glycosaminoglycan chains
301(1)
Bacterial cell walls are made of peptidoglycan
302
Box 11-A Biochemistry Note Cellulosic Biofuel
297(4)
Box 11-B Biochemistry Note The ABO Blood Group System
301(2)
Box 11-C Biochemistry Note Antibiotics and Bacterial Cell Walls
303(5)
part three Metabolism
12 Metabolism And Bioenergetics
308(30)
12-1 Food and Fuel
309(5)
Cells take up the products of digestion
309(3)
Monomers are stored as polymers
312(1)
Fuels are mobilized as needed
312(2)
12-2 Metabolic Pathways
314(9)
Some major metabolic pathways share a few common intermediates
315(1)
Many metabolic pathways include oxidation-reduction reactions
316(2)
Metabolic pathways are complex
318(2)
Human metabolism depends on vitamins
320(3)
12-3 Free Energy Changes in Metabolic Reactions
323(15)
The free energy change depends on reactant concentrations
323(2)
Unfavorable reactions are coupled to favorable reactions
325(3)
Free energy can take different forms
328(2)
Regulation occurs at the steps with the largest free energy changes
330
Box 12-A Biochemistry Note Dietary Guidelines
311(8)
Box 12-B Biochemistry Note The Transcriptome, the Proteome, and the Metabolome
319(5)
Box 12-C Biochemistry Note What Is a Calorie?
324(4)
Box 12-D Biochemistry Note Powering Human Muscles
328(4)
Bioinformatics Project 6 Metabolic Enzymes, Microarrays, and Proteomics
332(6)
13 Glucose Metabolism
338(32)
13-1 Glycolysis
339(15)
Reactions 1--5 are the energy-investment phase of glycolysis
341(4)
Reactions 6--10 are the energy-payoff phase of glycolysis
345(5)
Pyruvate is converted to other substances
350(4)
13-2 Gluconeogenesis
354(3)
Four gluconeogenic enzymes plus some glycolytic enzymes convert pyruvate to glucose
355(1)
Gluconeogenesis is regulated at the fructose bisphosphatase step
356(1)
13-3 Glycogen Synthesis and Degradation
357(4)
Glycogen synthesis consumes the free energy of UTP
358(1)
Glycogen phosphorylase catalyzes glycogenolysis
359(2)
13-4 The Pentose Phosphate Pathway
361(9)
The oxidative reactions of the pentose phosphate pathway produce NAD PH
361(1)
Isomerization and interconversion reactions generate a variety of monosaccharides
362(1)
A summary of glucose metabolism
363
Box 13-A Biochemistry Note Catabolism of Other Sugars
349(3)
Box 13-B Clinical Connection Alcohol Metabolism
352(8)
Box 13-C Clinical Connection Glycogen Storage Diseases
360(10)
14 The Citric Acid Cycle
370(5)
14-1 The Pyruvate Dehydrogenase Reaction
371(3)
The pyruvate dehydrogenase complex contains multiple copies of three different enzymes
371(1)
Pyruvate dehydrogenase converts pyruvate to acetyl-CoA
372(2)
14-2 The Eight Reactions of the Citric Acid Cycle
374(1)
1 Citrate synthase adds an acetyl group to oxaloacetate
375(1)
2 Aconitase isomerizes citrate to isocitrate
376(1)
3 Isocitrate dehydrogenase releases the first CO2
377(1)
4 α-Ketoglutarate dehydrogenase releases the second CO2
378(1)
5 Succinyl-CoA synthetase catalyzes substrate-level phosphorylation
378(1)
6 Succinate dehydrogenase generates ubiquinol
379(1)
7 Fumarase catalyzes a hydration reaction
380(1)
8 Malate dehydrogenase regenerates oxaloacetate
380(14)
The citric acid cycle is an energy-generating catalytic cycle
380(1)
The citric acid cycle is regulated at three steps
381(1)
The citric acid cycle probably evolved as a synthetic pathway
382(2)
14-3 Anabolic and Catabolic Functions of the Citric Acid Cycle
384(10)
Citric acid cycle intermediates are precursors of other molecules
384(1)
Anaplerotic reactions replenish citric acid cycle intermediates
385
Box 14-A Clinical Connection Mutations in Citric Acid Cycle Enzymes
382(4)
Box 14-B Biochemistry Note The Glyoxylate Pathway
386(8)
15 Oxidative Phosphorylation
394(26)
15-1 The Thermodynamics of Oxidation-Reduction Reactions
395(4)
Reduction potential indicates a substance's tendency to accept electrons
396(1)
The free energy change can be calculated from the change in reduction potential
397(2)
15-2 Mitochondrial Electron Transport
399(9)
Mitochondrial membranes define two compartments
399(2)
Complex I transfers electrons from NADH to ubiquinone
401(2)
Other oxidation reactions contribute to the ubiquinol pool
403(1)
Complex III transfers electrons from ubiquinol to cytochrome c
403(3)
Complex IV oxidizes cytochrome C and reduces O02
406(2)
15-3 Chemiosmosis
408(2)
Chemiosmosis links electron transport and oxidative phosphorylation
408(1)
The proton gradient is an electrochemical gradient
409(1)
15-4 ATP Synthase
410(10)
ATP synthase rotates as it translocates protons
410(2)
The binding change mechanism explains how ATP is made
412(1)
The P: O ratio describes the stoichiometry of oxidative phosphorylation
412(1)
The rate of oxidative phosphorylation depends on the rate of fuel catabolism
413
Box 15-A Biochemistry Note Free Radicals and Aging
407(6)
Box 15-B Biochemistry Note Uncoupling Agents Prevent ATP Synthesis
413(7)
16 Photosynthesis
420(22)
16-1 Chloroplasts and Solar Energy
422(3)
Pigments absorb light of different wavelengths
422(2)
Light-harvesting complexes transfer energy to the reaction center
424(1)
16-2 The Light Reactions
425(7)
Photosystem II is a light-activated oxidation-reduction enzyme
425(1)
The oxygen-evolving complex of Photosystem II oxidizes water
426(2)
Cytochrome b6ƒ links Photosystems I and II
428(1)
A second photooxidation occurs at Photosystem I
428(3)
Chemiosmosis provides the free energy for ATP synthesis
431(1)
16-3 Carbon Fixation
432(10)
Rubisco catalyzes CO2 fixation
432(2)
The Calvin cycle rearranges sugar molecules
434(2)
The availability of light regulates carbon fixation
436(1)
Calvin cycle products are used to synthesize sucrose and starch
436
Box 16-A Biochemistry Note The C4 Pathway
433(9)
17 Lipid Metabolism
442(33)
17-1 Fatty Acid Oxidation
445(8)
Fatty acids are activated before they are degraded
445(1)
Each round of B oxidation has four reactions
446(3)
Degradation of unsaturated fatty acids requires isomerization and reduction
449(1)
Oxidation of odd-chain fatty acids yields propionyl-CoA
450(1)
Some fatty acid oxidation occurs in peroxisomes
450(3)
17-2 Fatty Acid Synthesis
453(10)
Acetyl-CoA carboxylase catalyzes the first step of fatty acid synthesis
454(1)
Fatty acid synthase catalyzes seven reactions
455(2)
Other enzymes elongate and desaturate newly synthesized fatty acids
457(2)
Fatty acid synthesis can be activated and inhibited
459(2)
Acetyl-CoA can be converted to ketone bodies
461(2)
17-3 Synthesis of Other Lipids
463(12)
Triacylglycerols and phospholipids are built from acyl-CoA groups
463(3)
Cholesterol synthesis begins with acetyl-CoA
466(1)
Cholesterol can be used in several ways
467(2)
A summary of lipid metabolism
469
Box 17-A Biochemistry Note Fats, Diet, and Heart Disease
458(2)
Box 17-B Clinical Connection Inhibitors of Fatty Acid Synthesis
460(15)
18 Nitrogen Metabolism
475(34)
18-1 Nitrogen Fixation and Assimilation
476(4)
Nitrogenase converts N2 to NH3
476(1)
Ammonia is assimilated by glutamine synthetase and glutamate synthase
477(1)
Transamination moves amino groups between compounds
478(2)
18-2 Amino Acid Biosynthesis
480(8)
Several amino acids are easily synthesized from common metabolites
481(1)
Amino acids with sulfur, branched chains, or aromatic groups are more difficult to synthesize
482(4)
Amino acids are the precursors of some signaling molecules
486(2)
18-3 Nucleotide Biosynthesis
488(6)
Purine nucleotide synthesis yields IMP and then AMP and GMP
488(1)
Pyrimidine nucleotide synthesis yields UTP and CTP
489(1)
Ribonucleotide reductase converts ribonucleotides to deoxyribonucleotides
490(1)
Thymidine nucleotides are produced by methylation
491(1)
Nucleotide degradation produces uric acid or amino acids
492(2)
18-4 Amino Acid Catabolism
494(4)
Amino acids are glucogenic, ketogenic, or both
494(4)
18-5 Nitrogen Disposal: The Urea Cycle
498(11)
Glutamate supplies nitrogen to the urea cycle
499(1)
The urea cycle consists of four reactions
499
Box 18-A Biochemistry Note Transaminases in the Clinic
480(4)
Box 18-B Biochemistry Note Glyphosate, the Most Popular Herbicide
484(3)
Box 18-C Biochemistry Note Nitric Oxide
487(10)
Box 18-D Biochemistry Note Inborn Errors of Metabolism
497(12)
19 Regulation Of Mammalian Fuel Metabolism
509(20)
19-1 Integration of Fuel Metabolism
510(5)
Organs are specialized for different functions
510(3)
Metabolites travel between organs
513(2)
19-2 Hormonal Control of Fuel Metabolism
515(5)
Insulin is released in response to glucose
515(1)
Insulin promotes fuel use and storage
516(1)
Glucagon and epinephrine trigger fuel mobilization
517(1)
Additional hormones influence fuel metabolism
518(1)
AMP-dependent protein kinase acts as a fuel sensor
519(1)
19-3 Disorders of Fuel Metabolism
520(9)
The body generates glucose and ketone bodies during starvation
520(1)
Obesity has multiple causes
521(1)
Diabetes is characterized by hyperglycemia
522(1)
The metabolic syndrome links obesity and diabetes
523
Box 19-A Clinical Connection Cancer Metabolism
512(1)
Box 19-B Biochemistry Note The Intestinal Microbiome Contributes to Metabolism
513(7)
Box 19-C Biochemistry Note Marasmus and Kwashiorkor
520(9)
part four Genetic Information
20 DNA Replication And Repair
529(32)
20-1 DNA Supercoiling
530(3)
Topoisomerases alter DNA supercoiling
531(2)
20-2 The DNA Replication Machinery
533(7)
Replication occurs in factories
533(1)
Helicases convert double-stranded DNA to single-stranded DNA
533(1)
DNA polymerase faces two problems
534(2)
DNA polymerases share a common structure and mechanism
536(1)
DNA polymerase proofreads newly synthesized DNA
537(1)
An RNase and a ligase are required to complete the lagging strand
538(2)
20-3 Telomeres
540(3)
Telomerase extends chromosomes
540(3)
Is telomerase activity linked to cell immortality?
543(1)
20-4 DNA Damage and Repair
543(9)
DNA damage is unavoidable
543(4)
Repair enzymes restore some types of damaged DNA
547(1)
Base excision repair corrects the most frequent DNA lesions
548(1)
Nucleotide excision repair targets the second most common form of DNA damage
549(1)
Double-strand breaks can be repaired by joining the ends
550(1)
Recombination also restores broken DNA molecules
551(1)
20-5 DNA Packaging
552(9)
The fundamental unit of DNA packaging is the nucleosome
552(1)
Histones are covalently modified
553(1)
DNA also undergoes covalent modification
554
Box 20-A Biochemistry Note HIV Reverse Transcriptase
541(3)
Box 20-B Clinical Connection Cancer Is a Genetic Disease
544(17)
21 Transcription And RNA
561(29)
21-1 Transcription Initiation
563(8)
Chromatin remodeling may precede
transcription
563(1)
Transcription begins at promoters
564(2)
Transcription factors recognize eukaryotic) promoters
566(1)
Enhancers and silencers act at a distance from the promoter
566(4)
Prokaryotic operons allow coordinated gene expression
570(1)
21-2 RNA Polymerase
571(5)
RNA polymerase is a processive enzyme
573(1)
Transcription elongation requires a conformational change in RNA polymerase
573(1)
Transcription is terminated in several ways
574(2)
21-3 RNA Processing
576(14)
Eukaryotic mRNAs receive a 5' cap and a 3' poly(A) tail
576(1)
Splicing removes introns from eukaryotic genes
576(3)
mRNA turnover and RNA interference limit gene expression
579(2)
rRNA and tRNA processing includes the addition, deletion, and modification of nucleotides
581
Box 21-A Biochemistry Note DNA Binding Proteins
567(15)
Box 21-B Biochemistry Note RNA: A Versatile Molecule
582(8)
22 Protein Synthesis
590(27)
22-1 tRNA Aminoacylation
592(4)
tRNA aminoacylation consumes ATP
593(1)
Some synthetases have proofreading activity
594(1)
tRNA anticodons pair with mRNA codons
594(2)
22-2 Ribosome Structure
596(3)
22-3 Translation
599(9)
Initiation requires an initiator tRNA
599(2)
The appropriate tRNAs are delivered to the ribosome during elongation
601(2)
The peptidyl transferase active site catalyzes peptide bond formation
603(3)
Release factors mediate translation termination
606(1)
Translation is efficient in vivo
606(2)
22-4 Post-translational Events
608(9)
Chaperones promote protein folding
608(1)
The signal recognition particle targets some proteins for membrane translocation
609(2)
Many proteins undergo covalent modification
611
Box 22-A Biochemistry Note The Genetic Code Expanded
595(9)
Box 22-B Biochemistry Note Antibiotic Inhibitors of Protein Synthesis
604(13)
Glossary 617(12)
Solutions 629
Answers To Practice Problems 1(1)
Answers To Clinical Connection Questions 1(1)
Index 1