Biochemistry (9th Edition)

Description

Lubert Stryer is Winzer Professor of Cell Biology, Emeritus, in the School of Medicine and Professor of Neurobiology, Emeritus, at Stanford University,where he has been on the faculty since 1976. He received his M.D. from Harvard Medical School. Professor Stryer has received many awards for his research on theinterplay of light and life, including the Eli Lilly Award for Fundamental Research in Biological Chemistry, the Distinguished Inventors Award of the IntellectualProperty Owners’ Association, and election to the National Academy of Sciences and the American Philosophical Society. He was awarded the National Medalof Science in 2006. The publication of his first edition of Biochemistry in 1975 transformed the teaching of biochemistry.

Key Features

• Achieve combines acclaimed automatically graded online homework with a powerful e-book and an extensive suite of engaging multimedia learning resources. Problems feature hints for when students get stuck, answer-specific feedback to help them learn from their mistakes, and solutions to reinforce what they’ve learned.
• LearningCurve: Adaptive quizzing to get students prepared for class.
• Practice/homework problems with signature hints, targeted feedback, and detailed solutions – In every question, help features are embedded to guide students through common misconceptions. Atkins’ problems directly link to both the complete text and the relevant section level.
• Metabolic Map: With this interactive tool, students can navigate and zoom between overviews and detailed views of the most commonly taught metabolic pathways. Embedded Tutorials take students through the pathways step by step. Assessment questions align with the interactive map to help students verify their understanding of the pathways and connections among the pathways. *Metabolic Pathways include: glycolysis, gluconeogenesis, the citric acid cycle, oxidative phosphorylation, the pentose phosphate pathway, fatty acid synthesis, the urea cycle, and ?oxidation.
• Living Figures. Molecules represented in text figures can be found in manipulatable format.
• Case Studies. Introduce students to a biochemical mystery and allow them to determine what investigations will solve it.
• Problem-Solving Videos. With diagrams, graphs, and narration, these videos walk students through problems on topics that typically prove difficult, helping them understand the right approach to the solution.
• Animated Technique Videos
• Clicker Questions for Think/Pair/Share Questions
• Integrated Text and Media
• Metabolic Map. EXPLORE icons throughout the text denote topics where students are encouraged to take visual tours through the Metabolic Map.
• NEW! Tagged Learning Objectives for resources included in Achieve and an instructor guide make finding and assigning problems by learning objective easy and efficient.
• Living Figures. The Living Figure icons
• Animated Technique Videos. Whenever an EOC problem refers to a technique for which we have an animation, there is a link to those animations in Achieve.
• Promote Effective Problem Solving
• Problem-Solving Practice. Every chapter of Biochemistry provides numerous opportunities for students to practice problem-solving skills and apply the concepts described in the text. End-of-chapter problems vary in presentation and degree of difficulty to accommodate different learning styles and to coach students to develop different ways of looking at problem solving.
• Specialized Problems. There are four categories of problems to address higher-level problem-solving skills: mechanism problems ask students to suggest or describe a chemical mechanism; data interpretation problems require students to draw conclusions from data taken from real research papers; chapter integration problems require students to connect concepts across chapters; and (NEW!) think/pair/share problems provide instructors with tools to use this cooperative learning technique to encourage critical thinking and problem solving.
• Tools and Resources for Active Learning
• NEW! Think/Pair/Share Questions. Found in every end-of-chapter problem set, these new questions are designed to facilitate group thinking and mo

New to this Edition

Biochemistry is now supported in Achieve, Macmillan’s new online learning platform, Achieve is the culmination of years of development work put toward creating the most powerful online learning tool for chemistry students.  Achieve includes an interactive e-Book as well as our renowned assessments and a variety of multimedia assets. Instructors can assign or download instructor resources and take advantage of powerful analytics and quick insights to inform teaching.

The new ninth edition of Berg, Biochemistry includes:

• New graphics, design, and art
  The design of this edition retains the clean, somewhat minimalist, look that has been a hallmark of the textbook since Lubert Stryer first wrote the book in the 1970s. But in this edition, the book has added some graphic punch through its color palette and careful use of icons and other design elements.
• Updated clinical and evolutionary insight icons.
  NEW Industry Insight icon, which sits next to text that describes advances and research in areas like drug development, medicine, renewable energy, and sensor technology (Chapters 28, 14, 5, and 6, respectively).
• Many elements, like cell membranes, have been revised in every piece of art where they appear, again, to refresh and modernize the look of the textbook.
• New learning objectives
  Each chapter opening page now includes a numbered list of learning objectives: statements that will help students organize their notes and assist their focus as they read through a chapter. To reinforce the connections between the chapter content and the learning objectives, the learning objectives are tied to some of the end-of-chapter problems.
• New end of chapter active learning exercises
• Biochemistry in Focus: Vignettes focused on Recent developments in biochemistry
• Chapter 5: Biofuel production from genetically engineered algae
• Chapter 8: The effect of temperature on enzymes and the color of Siamese cats
• Chapter 12: The curious case of cardiolipin;
• Chapter 17: New treatments for tuberculosis
• Chapter 20: Hummingbirds and the pentose phosphate pathway
• Chapter 21: McArdle disease and skeletal muscle glycogen phosphorylase
• Chapter 25:Uridine plays a role in caloric homeostsis
• Chapter 27: Exercise alters muscle and whole-body metabolism;Chapter 32: Regulating gene expression through proteolysis
• Problem-Solving Strategies Unpack one or two problems so that students can see step-by-step how to solve complex, often multi-part, biochemistry problems.
• Chapters 15–27: These strategies focus on the core metabolism chapters
• Chapters 8, 9, and 10: introduction to enzymes
• NEW Think/Pair/Share. End of Chapter problems designed to be more open-ended and to require students to analyze and synthesize information from each chapter. The questions will work well as in-class activities and as small-group assignments either in or out of class using SaplingPlus.
• New scientific content
  The authors have updated every chapter based on the latest basic and biomedical research, agricultural developments, and industrial breakthroughs. For example, techniques like mass spectrometry and cryo-electron microscopy are revealing that for many metabolic pathways or major parts of them, the involved enzymes actually form enormous enzyme complexes (see, for example, Section 16.1 [glycolysis], Section 17.2 [citric acid cycle], and Section 18.3 [oxidative phosphorylation]). These large structures facilitate the transfer of reaction intermediates, reduce undesirable side reactions, and enhance the catalytic properties of the enzymes.
• The chapter on drug development has been revised and moved from its position at the end of the book to Chapter 28. Moving the drug development chapter near the end of the metabolism section highlights the importance of understanding the intricacies of metabolic pathways and the importance of developing drugs to combat disease and promote health.

Table of Contents

1. Part I THE MOLECULAR DESIGN OF LIFE
   Chapter 1 Biochemistry: An Evolving Science
   1.1 Biochemical Unity Underlies Biological Diversity
   1.2 DNA Illustrates the Interplay Between Form and Function
   DNA is constructed from four building blocks
   Two single strands of DNA combine to form a double helix
   DNA structure explains heredity and the storage of information
   1.3 Concepts from Chemistry Explain the Properties of Biological Molecules
   The formation of the DNA double helix as a key example
   The double helix can form from its component strands
   Covalent and noncovalent bonds are important for the structure and stability of biological molecules
   The double helix is an expression of the rules of chemistry
   The laws of thermodynamics govern the behavior of biochemical systems
   Heat is released in the formation of the double helix
   Acid–base reactions are central in many biochemical processes
   Acid–base reactions can disrupt the double helix
   Buffers regulate pH in organisms and in the laboratory
   1.4 The Genomic Revolution Is Transforming Biochemistry, Medicine, and Other Fields
   Genome sequencing has transformed biochemistry and other fields
   Environmental factors influence human biochemistry
   Genome sequences encode proteins and patterns of expression
   APPENDIX  Visualizing Molecular Structures: Small Molecules
   APPENDIX  Functional Groups
2. Chapter 2 Protein Composition and Structure
   2.1 Proteins Are Built from a Repertoire of 20 Amino Acids
   2.2 Primary Structure: Amino Acids Are Linked by Peptide Bonds to Form Polypeptide Chains
   Proteins have unique amino acid sequences specified by genes
   Polypeptide chains are flexible yet conformationally restricted
   2.3 Secondary Structure: Polypeptide Chains Can Fold into Regular Structures Such As the Alpha Helix, the Beta Sheet, and Turns and Loops
   The alpha helix is a coiled structure stabilized by intrachain hydrogen bonds
   Beta sheets are stabilized by hydrogen bonding between polypeptide strands
   Polypeptide chains can change direction by making reverse turns and loops
   2.4 Tertiary Structure: Proteins Can Fold into Globular or Fibrous Structures
   Fibrous proteins provide structural support for cells and tissues
   2.5 Quaternary Structure: Polypeptide Chains Can Assemble into Multisubunit Structures
   2.6 The Amino Acid Sequence of a Protein Determines Its Three-Dimensional Structure
   Amino acids have different propensities for forming < helices, ® sheets, and turns
   Protein folding is a highly cooperative process
   Proteins fold by progressive stabilization of intermediates rather than by random search
   Prediction of three-dimensional structure from sequence remains a great challenge
   Some proteins are inherently unstructured and can exist in multiple conformations
   Protein misfolding and aggregation are associated with some neurological diseases
   Posttranslational modifications confer new capabilities to proteins
   APPENDIX  Visualizing Molecular Structures: Proteins
3. Chapter 3 Exploring Proteins and Proteomes
   3.1 The Purification of Proteins Is an Essential First Step in Understanding Their Function
   The assay: How do we recognize the protein that we are looking for?
   Proteins must be released from the cell to be purified
   Proteins can be purified according to solubility, size, charge, and binding affinity
   Proteins can be separated by gel electrophoresis and displayed
   A protein purification scheme can be quantitatively evaluated
   Ultracentrifugation is valuable for separating biomolecules and determining their masses
   Protein purification can be made easier with the use of recombinant DNA technology
   3.2 Immunology Provides Important Techniques with Which to Investigate Proteins
   Antibodies to specific proteins can be generated
   Monoclonal antibodies with virtually any desired specificity can be readily prepared
   Proteins can be detected and quantified by using an enzyme-linked immunosorbent assay
   Western blotting permits the detection of proteins separated by gel electrophoresis
   Co-immunoprecipitation enables the identification of binding partners of a protein
   Fluorescent markers make the visualization of proteins in the cell possible
   3.3 Mass Spectrometry Is a Powerful Technique for the Identification of Peptides and Proteins
   Peptides can be sequenced by mass spectrometry
   Proteins can be specifically cleaved into small peptides to facilitate analysis
   Genomic and proteomic methods are complementary
   The amino acid se