Microbiology, 2021

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274 7 • Microbial Biochemistry shape of a protein is critical to its function. For example, in the process of biological nitrogen fixation (see Biogeochemical Cycles), soil microorganisms collectively known as rhizobia symbiotically interact with roots of legume plants such as soybeans, peanuts, or beans to form a novel structure called a nodule on the plant roots. The plant then produces a carrier protein called leghemoglobin, a protein that carries nitrogen or oxygen. Leghemoglobin binds with a very high affinity to its substrate oxygen at a specific region of the protein where the shape and amino acid sequence are appropriate (the active site). If the shape or chemical environment of the active site is altered, even slightly, the substrate may not be able to bind as strongly, or it may not bind at all. Thus, for the protein to be fully active, it must have the appropriate shape for its function. Protein structure is categorized in terms of four levels: primary, secondary, tertiary, and quaternary. The primary structure is simply the sequence of amino acids that make up the polypeptide chain. Figure 7.19 depicts the primary structure of a protein. The chain of amino acids that defines a protein’s primary structure is not rigid, but instead is flexible because of the nature of the bonds that hold the amino acids together. When the chain is sufficiently long, hydrogen bonding may occur between amine and carbonyl functional groups within the peptide backbone (excluding the R side group), resulting in localized folding of the polypeptide chain into helices and sheets. These shapes constitute a protein’s secondary structure. The most common secondary structures are the α-helix and β- pleated sheet. In the α-helix structure, the helix is held by hydrogen bonds between the oxygen atom in a carbonyl group of one amino acid and the hydrogen atom of the amino group that is just four amino acid units farther along the chain. In the β-pleated sheet, the pleats are formed by similar hydrogen bonds between continuous sequences of carbonyl and amino groups that are further separated on the backbone of the polypeptide chain (Figure 7.20). The next level of protein organization is the tertiary structure, which is the large-scale three-dimensional shape of a single polypeptide chain. Tertiary structure is determined by interactions between amino acid residues that are far apart in the chain. A variety of interactions give rise to protein tertiary structure, such as disulfide bridges, which are bonds between the sulfhydryl (–SH) functional groups on amino acid side groups; hydrogen bonds; ionic bonds; and hydrophobic interactions between nonpolar side chains. All these interactions, weak and strong, combine to determine the final three-dimensional shape of the protein and its function (Figure 7.21). The process by which a polypeptide chain assumes a large-scale, three-dimensional shape is called protein folding. Folded proteins that are fully functional in their normal biological role are said to possess a native structure. When a protein loses its three-dimensional shape, it may no longer be functional. These unfolded proteins are denatured. Denaturation implies the loss of the secondary structure and tertiary structure (and, if present, the quaternary structure) without the loss of the primary structure. Some proteins are assemblies of several separate polypeptides, also known as protein subunits. These proteins function adequately only when all subunits are present and appropriately configured. The interactions that hold these subunits together constitute the quaternary structure of the protein. The overall quaternary structure is stabilized by relatively weak interactions. Hemoglobin, for example, has a quaternary structure of four globular protein subunits: two α and two β polypeptides, each one containing an iron-based heme (Figure 7.22). Another important class of proteins is the conjugated proteins that have a nonprotein portion. If the conjugated protein has a carbohydrate attached, it is called a glycoprotein. If it has a lipid attached, it is called a lipoprotein. These proteins are important components of membranes. Figure 7.23 summarizes the four levels of protein structure. Access for free at openstax.org.
7.4 • Proteins 275 Figure 7.19 Research Institute) The primary structure of a protein is the sequence of amino acids. (credit: modification of work by National Human Genome Figure 7.20 The secondary structure of a protein may be an α-helix or a β-pleated sheet, or both.
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Microbiology SENIOR CONTRIBUTING AU
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OPENSTAX OpenStax provides free, pe
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Contents Preface 1 CHAPTER 1 An Inv
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9.2 Oxygen Requirements for Microbi
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18.1 Overview of Specific Adaptive
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Appendix C Metabolic Pathways 1155
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Preface 1 PREFACE Welcome to Microb
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Preface 3 that often confer critica
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Preface 5 further. Our features inc
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Preface 7 and science, and pursues
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CHAPTER 1 An Invisible World Figure
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1.1 • What Our Ancestors Knew 11
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1.2 • A Systematic Approach 17 Th
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1.2 • A Systematic Approach 19 Fi
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1.2 • A Systematic Approach 21 Ta
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1.3 • Types of Microorganisms 23
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1 • Summary 31 SUMMARY 1.1 What O
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1 • Review Questions 33 17. The p
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CHAPTER 2 How We See the Invisible
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2.1 • The Properties of Light 37
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2.1 • The Properties of Light 39
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2.2 • Peering Into the Invisible
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2.3 • Instruments of Microscopy 4
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2.4 • Staining Microscopic Specim
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2 • Review Questions 71 REVIEW QU
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CHAPTER 3 The Cell Figure 3.1 Micro
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3.1 • Spontaneous Generation 75 F
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3.2 • Foundations of Modern Cell
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3.3 • Unique Characteristics of P
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3.4 • Unique Characteristics of E
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3 • Summary 125 SUMMARY 3.1 Spont
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3 • Review Questions 127 3. Which
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3 • Review Questions 129 Critical
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CHAPTER 4 Prokaryotic Diversity Fig
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4.1 • Prokaryote Habitats, Relati
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4.2 • Proteobacteria 139 for or s
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4.2 • Proteobacteria 141 Class Al
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4.2 • Proteobacteria 143 Class Be
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4.2 • Proteobacteria 145 Figure 4
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4.2 • Proteobacteria 147 Class Ga
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4.3 • Nonproteobacteria Gram-Nega
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4.4 • Gram-Positive Bacteria 157
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4.6 • Archaea 167 The class Therm
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4.6 • Archaea 169 thus is a livin
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4 • Summary 171 SUMMARY 4.1 Proka
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4 • Review Questions 173 REVIEW Q
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4 • Review Questions 175 39. Expl
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CHAPTER 5 The Eukaryotes of Microbi
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5.1 • Unicellular Eukaryotic Para
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Figure 5.7 5.1 • Unicellular Euka
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5.2 • Parasitic Helminths 193 hel
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5.2 • Parasitic Helminths 195 Fig
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5.2 • Parasitic Helminths 197 Fig
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5.2 • Parasitic Helminths 199 MIC
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5.3 • Fungi 201 Figure 5.25 Multi
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5.3 • Fungi 203 Figure 5.27 zygos
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5.3 • Fungi 205 diploid stages (F
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5.3 • Fungi 207 Figure 5.32 prese
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5.3 • Fungi 209 MICRO CONNECTIONS
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5.4 • Algae 211 and other photosy
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5.5 • Lichens 213 Figure 5.37 Chl
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5.5 • Lichens 215 marina. (b) Thi
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5 • Review Questions 217 REVIEW Q
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CHAPTER 6 Acellular Pathogens Figur
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6.1 • Viruses 221 assembly of vir
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Page 267 and 268: 6 • Summary 253 SUMMARY 6.1 Virus
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Page 273 and 274: 7.1 • Organic Molecules 259 Figur
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Page 281 and 282: 7.3 • Lipids 267 Figure 7.11 Star
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8 • Review Questions 325 4. To wh
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8 • Review Questions 327 Matching
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CHAPTER 9 Microbial Growth Figure 9
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9.1 • How Microbes Grow 331 and a
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9.1 • How Microbes Grow 333 The G
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9.1 • How Microbes Grow 335 Susta
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9.1 • How Microbes Grow 337 chang
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9.1 • How Microbes Grow 339 Figur
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9.1 • How Microbes Grow 341 trans
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9.1 • How Microbes Grow 343 micro
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9.2 • Oxygen Requirements for Mic
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9.3 • The Effects of pH on Microb
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9.4 • Temperature and Microbial G
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9.4 • Temperature and Microbial G
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9.5 • Other Environmental Conditi
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9.6 • Media Used for Bacterial Gr
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9 • Summary 361 SUMMARY 9.1 How M
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9 • Review Questions 363 7. Filam
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9 • Review Questions 365 Matching
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9 • Review Questions 367 Critical
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CHAPTER 10 Biochemistry of the Geno
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10.1 • Using Microbiology to Disc
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10.2 • Structure and Function of
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10 • Summary 401 SUMMARY 10.1 Usi
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10 • Review Questions 403 3. Whic
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10 • Review Questions 405 Short A
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CHAPTER 11 Mechanisms of Microbial
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11.1 • The Functions of Genetic M
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11.2 • DNA Replication 411 Figure
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11.2 • DNA Replication 413 Figure
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11.2 • DNA Replication 415 strand
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11.2 • DNA Replication 417 telome
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11.3 • RNA Transcription 419 Figu
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11.3 • RNA Transcription 421 the
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11.4 • Protein Synthesis (Transla
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11.5 • Mutations 429 Effects of M
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11.5 • Mutations 431 In recent ye
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11.5 • Mutations 433 Figure 11.20
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11.5 • Mutations 435 formation of
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11.6 • How Asexual Prokaryotes Ac
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11.7 • Gene Regulation: Operon Th
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11 • Summary 457 SUMMARY 11.1 The
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11 • Summary 459 undamaged DNA st
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11 • Review Questions 461 11. Whi
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11 • Review Questions 463 46. ___
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71. The following figure is from Mo
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CHAPTER 12 Modern Applications of M
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12.1 • Microbes and the Tools of
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12.2 • Visualizing and Characteri
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12.3 • Whole Genome Methods and P
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12.3 • Whole Genome Methods and P
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12.4 • Gene Therapy 499 Figure 12
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12.4 • Gene Therapy 501 overall w
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12 • Summary 503 SUMMARY 12.1 Mic
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12 • Review Questions 505 11. The
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CHAPTER 13 Control of Microbial Gro
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13.1 • Controlling Microbial Grow
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13.2 • Using Physical Methods to
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13.3 • Using Chemicals to Control
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13.4 • Testing the Effectiveness
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13 • Summary 553 commonly used to
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13 • Review Questions 555 12. Ble
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CHAPTER 14 Antimicrobial Drugs Figu
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14.1 • History of Chemotherapy an
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14.1 • History of Chemotherapy an
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14.2 • Fundamentals of Antimicrob
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14.2 • Fundamentals of Antimicrob
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14.3 • Mechanisms of Antibacteria
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14.4 • Mechanisms of Other Antimi
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14.5 • Drug Resistance 591 Common
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14.5 • Drug Resistance 593 negati
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14.5 • Drug Resistance 595 Clavul
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14.7 • Current Strategies for Ant
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14.7 • Current Strategies for Ant
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14 • Summary 605 cells. • Becau
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14 • Review Questions 609 50. Why
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CHAPTER 15 Microbial Mechanisms of
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15.1 • Characteristics of Infecti
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15.2 • How Pathogens Cause Diseas
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15.3 • Virulence Factors of Bacte
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15.4 • Virulence Factors of Eukar
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15.4 • Virulence Factors of Eukar
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15 • Review Questions 647 protect
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15 • Review Questions 649 Critica
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CHAPTER 16 Disease and Epidemiology
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16.1 • The Language of Epidemiolo
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16.1 • The Language of Epidemiolo
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16.2 • Tracking Infectious Diseas
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16.3 • Modes of Disease Transmiss
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16.4 • Global Public Health 673 C
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16.4 • Global Public Health 675 S
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16 • Summary 677 SUMMARY 16.1 The
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16 • Review Questions 679 Matchin
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16 • Review Questions 681 20. Wha
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CHAPTER 17 Innate Nonspecific Host
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17.1 • Physical Defenses 685 Over
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17.1 • Physical Defenses 687 know
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17.1 • Physical Defenses 689 Figu
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17.2 • Chemical Defenses 691 Phys
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17.2 • Chemical Defenses 693 sali
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17.2 • Chemical Defenses 695 prod
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17.2 • Chemical Defenses 697 Figu
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17.2 • Chemical Defenses 699 Clin
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17.3 • Cellular Defenses 701 Hema
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17.3 • Cellular Defenses 703 stra
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17.3 • Cellular Defenses 705 Clin
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17.3 • Cellular Defenses 707 Figu
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17.4 • Pathogen Recognition and P
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17.4 • Pathogen Recognition and P
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17.5 • Inflammation and Fever 713
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17 • Summary 719 SUMMARY 17.1 Phy
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17 • Review Questions 721 8. Hist
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17 • Review Questions 723 Short A
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CHAPTER 18 Adaptive Specific Host D
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18.1 • Overview of Specific Adapt
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18.2 • Major Histocompatibility C
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18.3 • T Lymphocytes and Cellular
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18.4 • B Lymphocytes and Humoral
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18.4 • B Lymphocytes and Humoral
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18.5 • Vaccines 751 pathogen—bu
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18.5 • Vaccines 753 Eye on Ethics
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18.5 • Vaccines 755 for Disease C
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18.5 • Vaccines 757 Classes of Va
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18 • Summary 759 SUMMARY 18.1 Ove
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18 • Review Questions 761 5. MHC
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18 • Review Questions 763 20. Mat
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CHAPTER 19 Diseases of the Immune S
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19.1 • Hypersensitivities 767 Fig
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19.1 • Hypersensitivities 769 bin
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19.1 • Hypersensitivities 771 mec
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19.1 • Hypersensitivities 775 CHE
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19.1 • Hypersensitivities 777 Cli
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19.1 • Hypersensitivities 779 MIC
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19.2 • Autoimmune Disorders 783 t
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19.2 • Autoimmune Disorders 785 F
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19.2 • Autoimmune Disorders 787 M
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19.2 • Autoimmune Disorders 789 F
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19.3 • Organ Transplantation and
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19.4 • Immunodeficiency 793 and m
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19.4 • Immunodeficiency 795 CHECK
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19.5 • Cancer Immunobiology and I
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19 • Summary 799 SUMMARY 19.1 Hyp
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19 • Review Questions 801 13. All
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CHAPTER 20 Laboratory Analysis of t
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20.1 • Polyclonal and Monoclonal
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20.2 • Detecting Antigen-Antibody
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20.3 • Agglutination Assays 823 a
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20.3 • Agglutination Assays 825 F
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20.3 • Agglutination Assays 827 e
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20.3 • Agglutination Assays 829 s
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20.4 • EIAs and ELISAs 831 Mechan
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20.4 • EIAs and ELISAs 833 Figure
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20.4 • EIAs and ELISAs 837 • Wh
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20.5 • Fluorescent Antibody Techn
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20 • Review Questions 849 20.4 EI
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20 • Review Questions 851 15. Sup
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CHAPTER 21 Skin and Eye Infections
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21.1 • Anatomy and Normal Microbi
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21.2 • Bacterial Infections of th
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21.3 • Viral Infections of the Sk
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21.3 • Viral Infections of the Sk
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21.4 • Mycoses of the Skin 881 se
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21.4 • Mycoses of the Skin 883 fr
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21.4 • Mycoses of the Skin 885 Fi
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21.5 • Protozoan and Helminthic I
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21.5 • Protozoan and Helminthic I
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21 • Summary 891 SUMMARY 21.1 Ana
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CHAPTER 22 Respiratory System Infec
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22.4 • Respiratory Mycoses 931 ha
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22.4 • Respiratory Mycoses 933 Fi
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22.4 • Respiratory Mycoses 935 re
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Figure 22.29 22.4 • Respiratory M
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22 • Review Questions 939 200 vir
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CHAPTER 23 Urogenital System Infect
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23.5 • Fungal Infections of the R
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23.6 • Protozoan Infections of th
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23 • Summary 975 SUMMARY 23.1 Ana
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CHAPTER 24 Digestive System Infecti
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24.2 • Microbial Diseases of the
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24.4 • Viral Infections of the Ga
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24.6 • Helminthic Infections of t
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24 • Summary 1033 SUMMARY 24.1 An
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CHAPTER 25 Circulatory and Lymphati
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25.1 • Anatomy of the Circulatory
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25.1 • Anatomy of the Circulatory
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25.3 • Viral Infections of the Ci
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Figure 25.26 25.3 • Viral Infecti
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25.4 • Parasitic Infections of th
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25 • Review Questions 1089 • To
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25 • Review Questions 1091 Critic
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CHAPTER 26 Nervous System Infection
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26.1 • Anatomy of the Nervous Sys
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26.1 • Anatomy of the Nervous Sys
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26.2 • Bacterial Diseases of the
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26.3 • Acellular Diseases of the
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Figure 26.19 26.3 • Acellular Dis
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26.4 • Fungal and Parasitic Disea
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26 • Review Questions 1133 are fa
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26 • Review Questions 1135 Matchi
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26 • Review Questions 1137 59. Th
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A • Fundamentals of Physics and C
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B • Mathematical Basics 1149 APPE
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B • Mathematical Basics 1151 Mult
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B • Mathematical Basics 1153 The
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C • Metabolic Pathways 1155 APPEN
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C • Metabolic Pathways 1157 Entne
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C • Metabolic Pathways 1159 Figur
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C • Metabolic Pathways 1161 Elect
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APPENDIX D Taxonomy of Clinically R
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D • Taxonomy of Clinically Releva
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E • Glossary 1177 APPENDIX E Glos
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E • Glossary 1179 destruction by
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E • Glossary 1181 pollutants from
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E • Glossary 1183 chromosome disc
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E • Glossary 1185 cysts are forme
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E • Glossary 1187 occurring ectop
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E • Glossary 1189 molecules of DN
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E • Glossary 1191 glycoprotein co
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E • Glossary 1193 image point is
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E • Glossary 1195 discontinuously
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E • Glossary 1197 infection cause
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E • Glossary 1199 target cells by
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E • Glossary 1201 intact ribosome
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E • Glossary 1203 point source sp
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E • Glossary 1205 complexes forme
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E • Glossary 1207 antibody is fir
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E • Glossary 1209 the number of c
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E • Glossary 1211 the reciprocal
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E • Glossary 1213 vector animal (
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1215 ANSWER KEY Chapter 1 1. D 2. D
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1217 B 18. A, C, B 19. peristalsis
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Index 1219 INDEX Symbols +ssRNA 237
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Index 1221 antigen-presenting cells
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Index 1223 Bordetella 142 Bordetell
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Index 1225 chromosomes 372, 394 chr
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Index 1227 de Duve 113 dead zone 35
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Index 1229 Enteroinvasive E. coli (
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Index 1231 Gardnerella vaginalis 47
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Index 1233 shunt 298 Hfr cell 443 H
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Index 1235 iron lungs 1118 iron-sul
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Index 1237 maturation 230 mature na
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Index 1239 Health 501 National Noti
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Index 1241 patterns (PAMPs) 710 pat
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Index 1243 primary lymphoid tissue
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Index 1245 596, 1048, 1051, 1051 ri
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Index 1247 sterilant 511, 541 steri
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Index 1249 toxigenicity 633 toxin 6
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Index 1251 water activity 522 water
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Microbiology, 2021

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