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Essential Biochemistry 5th Edition PDF

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Essential Biochemistry, 5th Edition 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. This revised edition 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.

Features of Essential Biochemistry 5th Edition PDF

Here’s a quick overview of the essential features of this book:

Table of Contents

Below is the complete table of contents offered inside Essential Biochemistry 5th Edition PDF:

Part 1 Foundations

1 The Chemical Basis of Life 1

1.1 What Is Biochemistry? 1

1.2 Biological Molecules 3

Cells contain four major types of biomolecules 3

There are three major kinds of biological polymers 6

Box 1.A Units Used in Biochemistry 7

1.3 Energy and Metabolism 10

Enthalpy and entropy are components of free energy 11

ΔG is less than zero for a spontaneous process 12

Life is thermodynamically possible 12

1.4 The Origin of Cells 14

Prebiotic evolution led to cells 15

Box 1.B How Does Evolution Work? 17

Eukaryotes are more complex than prokaryotes 17

The human body includes microorganisms 19

2 Aqueous Chemistry 27

2.1 Water Molecules and Hydrogen Bonds 27

Hydrogen bonds are one type of electrostatic force 29

Water dissolves many compounds 31

Box 2.A Why Do Some Drugs Contain Fluorine? 31

2.2 The Hydrophobic Effect 33

Amphiphilic molecules experience both hydrophilic interactions and the hydrophobic effect 35

The hydrophobic core of a lipid bilayer is a barrier to diffusion 35

Box 2.B Sweat, Exercise, and Sports Drinks 36

2.3 Acid–Base Chemistry 37

[H+] and [OH–] are inversely related 38

The pH of a solution can be altered 39

Box 2.C Atmospheric CO2 and Ocean Acidification 39

A pK value describes an acid’s tendency to ionize 40

The pH of a solution of acid is related to the pK 41

2.4 Tools and Techniques: Buffers 44

2.5 Clinical Connection: Acid–Base Balance in Humans 46

Part 2 Molecular Structure and Function

3 Nucleic Acid Structure and Function 57

3.1 Nucleotides 57

Nucleic acids are polymers of nucleotides 58

Some nucleotides have other functions 60

3.2 Nucleic Acid Structure 61

DNA is a double helix 62

RNA is single-stranded 64

Nucleic acids can be denatured and renatured 64

3.3 The Central Dogma 67

Box 3.A Replication, Mitosis, Meiosis, and Mendel’s Laws 67

DNA must be decoded 70

A mutated gene can cause disease 71

Genes can be altered 72

Box 3.B Genetically Modified Organisms 73

3.4 Genomics 74

The exact number of human genes is not known 75

Genome size varies 75

Genomics has practical applications 77

Box 3.C Viruses 78

4 Protein Structure 86

4.1 Amino Acids, the Building Blocks of Proteins 86

The 20 amino acids have different chemical properties 88

Box 4.A Does Chirality Matter? 89

Box 4.B Monosodium Glutamate 91

Peptide bonds link amino acids in proteins 91

The amino acid sequence is the first level of protein structure 94

4.2 Secondary Structure: The Conformation of the Peptide Group 95

The α helix exhibits a twisted backbone conformation 96

The β sheet contains multiple polypeptide strands 96

Proteins also contain irregular secondary structure 98

4.3 Tertiary Structure and Protein Stability 99

Proteins can be described in different ways 99

Globular proteins have a hydrophobic core 100

Protein structures are stabilized mainly by the hydrophobic effect 101

Box 4.C Thioester Bonds as Spring-Loaded Traps 103

Protein folding is a dynamic process 103

Box 4.D Baking and Gluten Denaturation 104

Disorder is a feature of many proteins 105

Protein functions may depend on disordered regions 106

4.4 Quaternary Structure 107

4.5 Clinical Connection: Protein Misfolding and Disease 109

4.6 Tools and Techniques: Analyzing Protein Structure 111

Chromatography takes advantage of a polypeptide’s unique properties 111

Mass spectrometry reveals amino acid sequences 114

Box 4.E Mass Spectrometry Applications 116

Protein structures are determined by NMR spectroscopy, X-ray crystallography, and cryo-electron microscopy 116

5 Protein Function 125

5.1 Myoglobin and Hemoglobin: Oxygen-Binding Proteins 126

Oxygen binding to myoglobin depends on the oxygen concentration 127

Myoglobin and hemoglobin are related by evolution 128

Oxygen binds cooperatively to hemoglobin 129

A conformational shift explains hemoglobin’s cooperative behavior 130

Box 5.A Carbon Monoxide Poisoning 130

H+ ions and bisphosphoglycerate regulate oxygen binding to hemoglobin in vivo 132

5.2 Clinical Connection: Hemoglobin Variants 134

5.3 Structural Proteins 136

Actin filaments are most abundant 137

Actin filaments continuously extend and retract 138

Tubulin forms hollow microtubules 139

Keratin is an intermediate filament 142

Collagen is a triple helix 144

Box 5.B Vitamin C Deficiency Causes Scurvy 144

Collagen molecules are covalently cross-linked 145

Box 5.C Bone and Collagen Defects 147

5.4 Motor Proteins 148

Myosin has two heads and a long tail 148

Myosin operates through a lever mechanism 150

Kinesin is a microtubule-associated motor protein 151

Box 5.D Myosin Mutations and Deafness 151

Kinesin is a processive motor 152

5.5 Antibodies 154

Immunoglobulin G includes two antigen-binding sites 154

B lymphocytes produce diverse antibodies 156

Researchers take advantage of antibodies’ affinity and specificity 157

6 How Enzymes Work 167

6.1 What Is an Enzyme? 167

Enzymes are usually named after the reaction they catalyze 170

6.2 Chemical Catalytic Mechanisms 171

A catalyst provides a reaction pathway with a lower activation energy barrier 173

Enzymes use chemical catalytic mechanisms 173

Box 6.A Depicting Reaction Mechanisms 175

The catalytic triad of chymotrypsin promotes peptide bond hydrolysis 177

6.3 Unique Properties of Enzyme Catalysts 180

Enzymes stabilize the transition state 180

Efficient catalysis depends on proximity and orientation effects 181

The active-site microenvironment promotes catalysis 182

6.4 Chymotrypsin in Context 183

Not all serine proteases are related by evolution 183

Enzymes with similar mechanisms exhibit different substrate specificity 184

Chymotrypsin is activated by proteolysis 185

Protease inhibitors limit protease activity 186

6.5 Clinical Connection: Blood Coagulation 187

7 Enzyme Kinetics and Inhibition 198

7.1 Introduction to Enzyme Kinetics 198

7.2 Derivation and Meaning of the Michaelis–Menten Equation 201

Rate equations describe chemical processes 201

The Michaelis–Menten equation is a rate equation for an enzyme-catalyzed reaction 202

KM is the substrate concentration at which velocity is half-maximal 204

The catalytic constant describes how quickly an enzyme can act 204

kcat/KM indicates catalytic efficiency 205

KM and Vmax are experimentally determined 205

Not all enzymes fit the simple Michaelis–Menten model 207

7.3 Enzyme Inhibition 209

Some inhibitors act irreversibly 209

Competitive inhibition is the most common form of reversible enzyme inhibition 210

Transition state analogs inhibit enzymes 212

Other types of inhibitors affect Vmax 213

Box 7.A Inhibitors of HIV Protease 214

Allosteric enzyme regulation includes inhibition and activation 216

Several factors may influence enzyme activity 219

7.4 Clinical Connection: Drug Development 219

8 Lipids and Membranes 234

8.1 Lipids 234

Fatty acids contain long hydrocarbon chains 235

Box 8.A Omega-3 Fatty Acids 236

Some lipids contain polar head groups 237

Lipids perform a variety of physiological functions 239

Box 8.B The Lipid Vitamins A, D, E, and K 240

8.2 The Lipid Bilayer 241

The bilayer is a fluid structure 242

Natural bilayers are asymmetric 243

8.3 Membrane Proteins 244

Integral membrane proteins span the bilayer 245

An α helix can cross the bilayer 245

A transmembrane β sheet forms a barrel 246

Lipid-linked proteins are anchored in the membrane 246

8.4 The Fluid Mosaic Model 248

Membrane proteins have a fixed orientation 249

Lipid asymmetry is maintained by enzymes 250

9 Membrane Transport 258

9.1 The Thermodynamics of Membrane Transport 258

Ion movements alter membrane potential 259

Membrane proteins mediate transmembrane ion movement 260

9.2 Passive Transport 263

Porins are β barrel proteins 263

Ion channels are highly selective 264

Gated channels undergo conformational changes 265

Box 9.A Pores Can Kill 265

Aquaporins are water-specific pores 266

Some transport proteins alternate between conformations 268

9.3 Active Transport 269

The Na,K-ATPase changes conformation as it pumps ions across the membrane 269

ABC transporters mediate drug resistance 271

Secondary active transport exploits existing gradients 271

9.4 Membrane Fusion 272

SNAREs link vesicle and plasma membranes 273

Box 9.B Antidepressants Block Serotonin Transport 275

Endocytosis is the reverse of exocytosis 276

Autophagosomes enclose cell materials for degradation 277

Box 9.C Exosomes 278

10 Signaling 287

10.1 General Features of Signaling Pathways 287

A ligand binds to a receptor with a characteristic affinity 288

Most signaling occurs through two types of receptors 289

The effects of signaling are limited 290

10.2 G Protein Signaling Pathways 291

G protein–coupled receptors include seven transmembrane helices 292

The receptor activates a G protein 293

The second messenger cyclic AMP activates protein kinase A 294

Arrestin competes with G proteins 296

Signaling pathways must be switched off 296

The phosphoinositide signaling pathway generates two second messengers 297

Many sensory receptors are GPCRs 298

Box 10.A Opioids 299

10.3 Receptor Tyrosine Kinases 300

The insulin receptor dimer changes conformation 300

The receptor undergoes autophosphorylation 302

Box 10.B Cell Signaling and Cancer 303

10.4 Lipid Hormone Signaling 303

Eicosanoids are short-range signals 305

Box 10.C Inhibitors of Cyclooxygenase 306


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