Figure: 14-01 Title: A Comparison of the Components in Prokaryotic and Eukaryotic Ribosomes Caption: A comparison of the components in prokaryotic and eukaryotic ribosomes.

Figure: 14-02 Title: Ribonucleotides Caption: Ribonucleotides containing unusual nitrogenous bases found in transfer RNA.

Figure: 14-03 Title: Cloverleaf Model of Transfer RNA Caption: Holley’s two-dimensional cloverleaf model of transfer RNA. Black pegs represent nitrogenous bases.

Figure: 14-04 Title: A Three-dimensional Model of Transfer RNA Caption: A three-dimensional model of transfer RNA.

Figure: 14-05 Title: Steps Involved in Charging tRNA Caption: Steps involved in charging tRNA. The superscript x denotes that only the corresponding specific tRNA and specific aminoacyl tRNA synthetase enzyme are involved in the charging process for each amino acid.

Figure: 14-06a Title: Initiation of Translation Caption: Initiation of translation. The components are depicted at the left of the figure.

Figure: 14-06b Title: Initiation of Translation Caption: Initiation of translation. The components are depicted at the left of the figure.

Figure: 14-07a Title: Elongation Caption: Elongation of the growing polypeptide chain during translation.

Figure: 14-07b Title: Elongation Caption: Elongation of the growing polypeptide chain during translation.

Figure: 14-07c Title: Elongation Caption: Elongation of the growing polypeptide chain during translation.

Figure: 14-08 Title: Termination Caption: Termination of the process of translation.

Figure: 14-09a Title: Polyribosomes Caption: Polyribosomes as seen under the electron microscope. They were derived from rabbit reticulocytes engaged in the translation of hemoglobin mRNA. (Photo: from Rich et al. 1963. Reproduced by permission of the Cold Spring Harbor Laboratory Press Symp. 28 (1963) p. 273, Fig. 4D, © 1964)

Figure: 14-09b Title: Polyribosomes Caption: Polyribosomes as seen under the electron microscope. They were taken from giant salivary gland cells of the midgefly, Chironomus thummi. Note that the nascent polypeptide chain is apparent as it emerges from each ribosome. Its length increases as translation proceeds from left (5’) to right (3’) along the mRNA. (Photo: E. V. Kiseleva)

Figure: 14-10 Title: Metabolic Pathway Involving Phenylalanine and Tyrosine Caption: Metabolic pathway involving phenylalanine and tyrosine. Various metabolic blocks resulting from mutations lead to the disorders phenylketonuria, alkaptonuria, albinism, and tyrosinemia.

Figure: 14-11a Title: Nutritional Auxotrophic Mutation in Neurospora Caption: Induction, isolation, and characterization of a nutritional auxotrophic mutation in Neurospora. (a) Most conidia are not affected, but one conidium (shown in red) contains the mutation. In (b) and (c), the precise nature of the mutation is established and found to involve the biosynthesis of tyrosine.

Figure: 14-11b Title: Nutritional Auxotrophic Mutation in Neurospora Caption: Induction, isolation, and characterization of a nutritional auxotrophic mutation in Neurospora. (a) Most conidia are not affected, but one conidium (shown in red) contains the mutation. In (b) and (c), the precise nature of the mutation is established and found to involve the biosynthesis of tyrosine.

Figure: 14-11c Title: Nutritional Auxotrophic Mutation in Neurospora Caption: Induction, isolation, and characterization of a nutritional auxotrophic mutation in Neurospora. (a) Most conidia are not affected, but one conidium (shown in red) contains the mutation. In (b) and (c), the precise nature of the mutation is established and found to involve the biosynthesis of tyrosine.

Figure: 14-12 Title: Biosynthesis of Arginine in Neurospora Caption: Abbreviated pathway resulting in the biosynthesis of arginine in Neurospora.

Figure: 14-14a Title: Investigation of Hemoglobin Caption: Investigation of hemoglobin derived from HbAHbA and HbSHbS individuals by using electrophoresis, protein fingerprinting, and amino acid analysis. Hemoglobin from individuals with sickle-cell anemia (HbSHbS) (a) migrates differently in an electrophoretic field, (b) shows an altered peptide in fingerprint analysis, and (c) shows an altered amino acid, valine, at the sixth position in the Beta chain. During electrophoresis, heterozygotes (HbAHbS) reveal both forms of hemoglobin.

Figure: 14-14b Title: Investigation of Hemoglobin Caption: Investigation of hemoglobin derived from HbAHbA and HbSHbS individuals by using electrophoresis, protein fingerprinting, and amino acid analysis. Hemoglobin from individuals with sickle-cell anemia (HbSHbS) (a) migrates differently in an electrophoretic field, (b) shows an altered peptide in fingerprint analysis, and (c) shows an altered amino acid, valine, at the sixth position in the Beta chain. During electrophoresis, heterozygotes (HbAHbS) reveal both forms of hemoglobin.

Figure: 14-15a Title: Chemical Structures and Designations of Amino Acids Caption: Chemical structures and designations of the 20 amino acids found in living organisms, divided into 4 major categories. Each amino acid has two abbreviations; that is, alanine is designated either ala or A (a universal nomenclature).

Figure: 14-15b Title: Chemical Structures and Designations of Amino Acids Caption: Chemical structures and designations of the 20 amino acids found in living organisms, divided into 4 major categories. Each amino acid has two abbreviations; that is, alanine is designated either ala or A (a universal nomenclature).

Figure: 14-15c Title: Chemical Structures and Designations of Amino Acids Caption: Chemical structures and designations of the 20 amino acids found in living organisms, divided into 4 major categories. Each amino acid has two abbreviations; that is, alanine is designated either ala or A (a universal nomenclature).

Figure: 14-15d Title: Chemical Structures and Designations of Amino Acids Caption: Chemical structures and designations of the 20 amino acids found in living organisms, divided into 4 major categories. Each amino acid has two abbreviations; that is, alanine is designated either ala or A (a universal nomenclature).

Figure: 14-16 Title: Peptide Bond Formation Caption: Peptide bond formation between two amino acids, resulting from a dehydration reaction.

Figure: 14-17 Title: Secondary Structure of Protein Caption: (a) The right-handed alpha helix, which represents one form of secondary structure of a polypeptide chain. (b) The beta-pleated sheet, an alternative form of secondary structure of polypeptide chains. To maintain clarity, not all atoms are shown.

Figure: 14-18 Title: Tertiary Structure of Protein Caption: The tertiary level of protein structure in a respiratory pigment, myoglobin. The bound oxygen atom is shown in red. (Horton et al., Principles of Biochemistry, 3rd ed. © 2002. Reprinted by permission of Prentice-Hall, Inc., Upper Saddle River, NJ)

Figure: 14-19 Title: Quaternary Structure of Protein Caption: The quaternary level of protein structure as seen in hemoglobin. Four chains (two alpha and two beta) interact with four heme groups to form the functional molecule.

Figure: 14-20 Title: Uncatalyzed Versus an Enzymatically Catalyzed Chemical Reaction Caption: Energy requirements of an uncatalyzed versus an enzymatically catalyzed chemical reaction. The energy of activation (Ea) necessary to initiate the reaction is substantially lower as a result of catalysis.

Figure: 14-21 Title: Exons of the LDL Receptor Protein Gene Caption: The 18 exons making up the gene encoding the LDL receptor protein are organized into five functional domains and one signal sequence.

Figure: 14-UN01 Title: Problems and Discussion Caption: Problems and Discussion question 35. Graph of Optional cleavage vs. Antisense oligonucleotide length

Figure: 14-T01 Title: Table 14-1 Caption: Various Protein Factors Involved During Translation in E. coli.