Biochemistry : concepts and connections

Biochemistry concepts and connections

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Bibliographic Details
Other Authors: Appling, Dean Ramsay, author (author), Anthony-Cahill, Spencer J., author, Mathews, Christopher K., 1937- author
Format: eBook
Language:Inglés
Published: Harlow, England : Pearson Education Limited [2019]
Edition:Second edition
Subjects:
Biochemistry.
Libros electrónicos.
See on Biblioteca Universitat Ramon Llull:https://discovery.url.edu/permalink/34CSUC_URL/1im36ta/alma991009632536806719
Table of Contents:
  • Cover
  • Title Page
  • Copyright Page
  • Brief Contents
  • Contents
  • Preface
  • Acknowledgments for the Global Edition
  • 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 Nonequilibrium Concentrations of Reactants and Products
  • Equilibrium, Le Chatelier's Principle, and the Standard State
  • Changes in Concentration and .G
  • .G versus .G°, 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
  • .G 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
  • Posttranslational 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 ß 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.

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