Biochemistry : concepts and connections / / Dean Ramsay Appling; Spencer J. Anthony-Cahill; Christopher K. Mathews

• Record Nr.: UNINA9910154761803321
• Autore: Appling Dean Ramsay
• Pubbl/distr/stampa: Harlow, England : , : Pearson Education Limited, , [2016]; ©2016
• ISBN: 1-292-11201-8
• Edizione: [Global edition.]
• Descrizione fisica: 1 online resource (925 pages) : color illustrations, photographs
• Collana: Always learning
• Disciplina: 572
• Soggetti: Biochemical genetics; Biochemistry; Metabolism
• Lingua di pubblicazione: Inglese
• Formato: Materiale a stampa
• Livello bibliografico: Monografia
• Note generali: Includes index.
• Nota di bibliografia: Includes bibliographical references and index.
• Nota di contenuto: Cover -- Title page -- Copyright page -- Brief contents -- Contents -- Preface -- About the Authors -- Tools of Biochemistry -- Foundation Figures -- Chapter 1 -- Biochemistry and the Language of Chemistry -- 1.1 The Science of Biochemistry -- The Origins of Biochemistry -- The Tools of Biochemistry -- Biochemistry as a Discipline and an Interdisciplinary Science -- 1.2 The Elements and Molecules of Living Systems -- The Chemical Elements of Cells and Organisms -- The Origin of Biomolecules and Cells -- The Complexity and Size of Biological Molecules -- The Biopolymers: Proteins, Nucleic Acids, and Carbohydrates -- Lipids and Membranes -- 1.3 Distinguishing Characteristics of Living Systems -- 1.4 The Unit of Biological Organization: The Cell -- 1.5 Biochemistry and the Information Explosion -- Chapter 2 -- The Chemical Foundation of Life: Weak Interactions in an Aqueous Environment -- 2.1 The Importance of Noncovalent Interactions in Biochemistry -- 2.2 The Nature of Noncovalent Interactions -- Charge-Charge Interactions -- Dipole and Induced-Dipole Interactions -- Van der Waals Interactions -- Hydrogen Bonds -- 2.3 The Role of Water in Biological Processes -- The Structure and Properties of Water -- Water as a Solvent -- Ionic Compounds in Aqueous Solution -- Hydrophilic Molecules in Aqueous Solution -- Hydrophobic Molecules in Aqueous Solution -- Amphipathic Molecules ; in Aqueous Solution -- 2.4 Acid-Base Equilibria -- Acids and Bases: Proton Donors and Acceptors -- Ionization of Water and the Ion Product -- The pH Scale and the Physiological pH Range -- Weak Acid and Base Equilibria: Ka and pKa -- Titration of Weak Acids: The Henderson-Hasselbalch Equation -- Buffer Solutions -- Molecules with Multiple Ionizing Groups -- 2.5 Interactions Between Macroions in Solution -- Solubility of Macroions and pH.; The Influence of Small Ions: Ionic Strength -- Tools Of Biochemistry 2A Electrophoresis and Isoelectric Focusing -- Foundation figure Biomolecules: Structure and Function -- Chapter 3 -- The Energetics of Life -- 3.1 Free Energy -- Thermodynamic Systems -- The First Law of Thermodynamics and Enthalpy -- The Driving Force for a Process -- Entropy -- The Second Law of Thermodynamics -- 3.2 Free Energy: The Second Law in Open Systems -- Free Energy Defined in Terms of Enthalpy and Entropy Changes in the System -- An Example of the Interplay of Enthalpy and Entropy: The Transition Between Liquid Water and Ice -- The Interplay of Enthalpy and Entropy: A Summary -- Free Energy and Useful Work -- 3.3 The Relationships Between Free Energy, the Equilibrium State, and Non-Equilibrium Concentrations of Reactants and Products -- Equilibrium, Le Chatelier's Principle, and the Standard State -- Changes in Concentration and ΔG -- ΔG versus ΔG°, Q versus K, and Homeostasis versus Equilibrium -- Water, H+ in Buffered Solutions, and the "Biochemical Standard State -- 3.4 Free Energy in Biological Systems -- Organic Phosphate Compounds as Energy Transducers -- Phosphoryl Group Transfer Potential -- Free Energy and Concentration Gradients: A Close Look at Diffusion Through a Membrane -- ΔG and Oxidation/Reduction Reactions in Cells -- Quantification of Reducing Power: Standard Reduction Potential -- Standard Free Energy Changes in Oxidation-Reduction Reactions -- Calculating Free Energy Changes for Biological Oxidations under Nonequilibrium Conditions -- A Brief Overview of Free Energy Changes in Cells -- Chapter 4 -- Nucleic Acids -- 4.1 Nucleic Acids-Informational Macromolecules -- The Two Types of Nucleic Acid: DNA and RNA -- Properties of the Nucleotides -- Stability and Formation of the Phosphodiester Linkage -- 4.2 Primary Structure of Nucleic Acids.; The Nature and Significance of Primary Structure -- DNA as the Genetic Substance: Early Evidence -- 4.3 Secondary and Tertiary Structures of Nucleic Acids -- The DNA Double Helix -- Data Leading Toward the Watson-Crick Double-Helix Model -- X-Ray Analysis of DNA Fibers -- Semiconservative Nature of DNA Replication -- Alternative Nucleic Acid Structures: B and A Helices -- DNA and RNA Molecules in Vivo -- DNA Molecules -- Circular DNA and Supercoiling -- Single-Stranded Polynucleotides -- 4.4 Alternative Secondary Structures of DNA -- Left-Handed DNA (Z-DNA) -- Hairpins and Cruciforms -- Triple Helices -- G-Quadruplexes -- 4.5 The Helix-to-Random Coil Transition: Nucleic Acid Denaturation -- 4.6 The Biological Functions of Nucleic Acids: A Preview of Genetic Biochemistry -- Genetic Information Storage: The Genome -- Replication: DNA to DNA -- Transcription: DNA to RNA -- Translation: RNA to Protein -- Tools Of Biochemistry 4A Manipulating DNA -- Tools Of Biochemistry 4B An Introduction to X-Ray Diffraction -- Chapter 5 -- Introduction to Proteins: The Primary Level of Protein Structure -- 5.1 Amino Acids -- Structure of the a-Amino Acids -- Stereochemistry of the a-Amino Acids -- Properties of Amino Acid Side Chains: Classes of a-Amino Acids -- Amino Acids with Nonpolar Aliphatic Side Chains -- Amino Acids with Nonpolar Aromatic Side Chains -- Amino Acids with Polar Side Chains -- Amino Acids with Positively Charged (Basic) Side Chains -- Amino Acids with Negatively Charged (Acidic) Side Chains -- Rare Genetically Encoded Amino Acids ; -- Modified Amino Acids -- 5.2 Peptides and the Peptide Bond -- The Structure of the Peptide Bond -- Stability and Formation of the Peptide Bond -- Peptides -- Polypeptides as Polyampholytes -- 5.3 Proteins: Polypeptides of Defined Sequence -- 5.4 From Gene to Protein -- The Genetic Code.; Post-translational Processing of Proteins -- 5.5 From Gene Sequence to Protein Function -- 5.6 Protein Sequence Homology -- Tools Of Biochemistry 5A Protein Expression and Purification -- Tools Of Biochemistry 5B Mass, Sequence, and Amino Acid Analyses of Purified Proteins -- Chapter 6 -- The Three-Dimensional Structure of Proteins -- 6.1 Secondary Structure: Regular Ways to Fold the Polypeptide Chain -- Theoretical Descriptions of Regular Polypeptide Structures -- a Helices and B Sheets -- Describing the Structures: Helices and Sheets -- Amphipathic Helices and Sheets -- Ramachandran Plots -- 6.2 Fibrous Proteins: Structural Materials of Cells and Tissues -- The Keratins -- Fibroin -- Collagen -- 6.3 Globular Proteins: Tertiary Structure and Functional Diversity -- Different Folding for Different Functions -- Different Modes of Display Aid Our Understanding of Protein Structure -- Varieties of Globular Protein Structure: Patterns of Main-Chain Folding -- 6.4 Factors Determining Secondary and Tertiary Structure -- The Information for Protein Folding -- The Thermodynamics of Folding -- Conformational Entropy -- Charge-Charge Interactions -- Internal Hydrogen Bonds -- Van der Waals Interactions -- The Hydrophobic Effect -- Disulfide Bonds and Protein Stability -- Prosthetic Groups, Ion-binding, and Protein Stability -- 6.5 Dynamics of Globular Protein Structure -- Kinetics of Protein Folding -- The "Energy Landscape" Model of Protein Folding -- Intermediate and Off-Pathway States in Protein Folding -- Chaperones Faciliate Protein Folding in Vivo -- Protein Misfolding and Disease -- 6.6 Prediction of Protein Secondary and Tertiary Structure -- Prediction of Secondary Structure -- Tertiary Structure Prediction: Computer Simulation of Folding -- 6.7 Quaternary Structure of Proteins.; Symmetry in Multisubunit Proteins: Homotypic Protein-Protein Interactions -- Heterotypic Protein-Protein Interactions -- Tools Of Biochemistry 6A Spectroscopic Methods for Studying Macromolecular Conformation in Solution -- Tools Of Biochemistry 6B Determining Molecular Masses and the Number of Subunits in a Protein Molecule -- Foundation figure Protein Structure and Function -- Chapter 7 -- Protein Function and Evolution -- 7.1 Binding a Specific Target: Antibody Structure and Function -- 7.2 The Adaptive Immune Response -- 7.3 The Structure of Antibodies -- 7.4 Antibody:Antigen Interactions -- Shape and Charge Complementarity -- Generation of Antibody Diversity -- 7.5 The Immunoglobulin Superfamily -- 7.6 The Challenge of Developing an AIDS Vaccine -- 7.7 Antibodies and Immunoconjugates as Potential Cancer Treatments -- 7.8 Oxygen Transport from Lungs to Tissues: Protein Conformational Change Enhances Function -- 7.9 The Oxygen Binding Sites in Myoglobin and Hemoglobin -- Analysis of Oxygen Binding by Myoglobin -- 7.10 The Role of Conformational Change in Oxygen Transport -- Cooperative Binding and Allostery -- Models for the Allosteric Change in Hemoglobin -- Changes in Hemoglobin Structure Accompanying Oxygen Binding -- A Closer Look at the Allosteric Change in Hemoglobin -- 7.11 Allosteric Effectors of Hemoglobin Promote Efficient Oxygen Delivery to Tissues -- Response to pH Changes: The Bohr Effect -- Carbon Dioxide Transport -- Response to Chloride Ion at the a-Globin N-Terminus -- 2,3-Bisphosphoglycerate -- 7.12 Myoglobin and Hemoglobin as Examples of the Evolution of Protein Function -- The Structure of Eukaryotic Genes: Exons and Introns -- ; 7.13 Mechanisms of Protein Mutation -- Substitution of DNA Nucleotides -- Nucleotide Deletions or Insertions -- Gene Duplications and Rearrangements.; Evolution of the Myoglobin-Hemoglobin Family of Proteins.
• Sommario/riassunto: For one or two semester biochemistry courses (science majors). A highly visual, precise and fresh approach to guide today's mixed-science majors to a deeper understanding of biochemistry Biochemistry: Concepts and Connections engages students in the rapidly evolving field of biochemistry, better preparing them for the challenges of 21st century science through quantitative reasoning skills and a rich, chemical perspective on biological processes. This concise first edition teaches mixed-science-majors the chemical logic underlying the mechanisms, pathways, and processes in living cells through groundbreaking biochemical art and a clear narrative that illustrates biochemistry's relation to all other life sciences. Integration of biochemistry's experimental underpinnings alongside the presentation of modern techniques encourages students to appreciate and consider how their understanding of biochemistry can and will contribute to solving problems in medicine, agricultural sciences, environmental sciences, and forensics. The text is fully integrated with MasteringChemistry to provide support for students before, during, and after class. Highlights include interactive animations and tutorials based on the textbook's biochemical art program and Foundation Figures to help students visualize complex processes, apply, and test conceptual understanding as well as quantitative reasoning. MasteringChemistry not included. Students, if MasteringChemistry is a recommended/mandatory component of the course, please ask your instructor for the correct ISBN and course ID. MasteringChemistry should only be purchased when required by an instructor. Instructors, contact your Pearson representative for more information. Also available with MasteringChemistry® MasteringChemistry from Pearson is the leading online; homework, tutorial, and assessment system, designed to improve results by engaging students before, during, and after class with powerful content. Instructors ensure students arrive prepared by assigning interaction with relevant biochemical concepts before class, and encourage critical thinking, visualization, and retention with in-class resources such as Learning Catalytics™. Students can further master concepts after class by interacting with biochemistry animations, problem sets, and tutorial assignments that provide hints and answer-specific feedback. The Mastering gradebook records scores for all automatically graded assignments in one place, while diagnostic tools give instructors access to rich data to assess student understanding and misconceptions. Mastering brings learning full circle by continuously adapting to each student and making learning more personal than ever-before, during, and after class. &nbsp.