Biochemistry: A Short Course (4th Edition)

Description

Derived from the classic text originated by Lubert Stryer and continued by John Tymoczko and Jeremy Berg, Biochemistry: A Short Course focuses on the major topics taught in a one-semester biochemistry course. With its brief chapters and relevant examples, this thoroughly updated new edition helps students see the connections between the biochemistry they are studying and their own lives.

The focus of the 4th edition has been around:

Biochemistry: A Short Course 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

• Tools and Resources for Active Learning
  A number of new features are designed to help instructors create a more active environment in the classroom. Tools and resources are provided within the text, Achieve and instructor resources.
• Extensive Problem-Solving Tools
  A variety of end of chapter problems promote understanding of single concept and multi-concept problems. Built-in assessments help students keep on track with reading and become proficient problem solvers with the help and guidance of hints and targeted feedback—ensuring every problem counts as a true learning experience. Unique case studies and new Think/Pair/Share Problems help provide application and relevance, as well as a vehicle for active learning.

New to this Edition

Biochemistry: A Short Course 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 fourth edition of Tymoczko/ Berg, Biochemistry: A Short Course  takes into account recent discoveries and advances that have changed how we think about the fundamental concepts in biochemistry and human health and includes the following updates:

• Refreshed design for 4e that includes newly styled icons and color scheme. Also includes some new chapter opening photos.
• Thoroughly updated text and figures based on latest research and discoveries in biochemistry and related fields.
• NEW Industry Insights and a new icon focusing on up-to-date research and technologies. Some of the Clinical and Biological Insights content has been updated to address current research.
• NEW Biochemistry in Focus appendix added to the EOC material in most every chapter—designed to explore the application of chapter content to an engaging example, such as disease.
• Updated margin notes including new Quick Quizzes, Nutrition Facts, and Did You Know?

The Latest Discoveries in Biochemistry Research
The study of biochemistry is closely allied with many other types of biological
and biomedical research. The latest discoveries, hypotheses, and research techniques
in biochemistry and allied fields are presented, including the following:

• ATP may have roles other than in energy and signal transduction (Chapter 15)
• Most of the electron transport chain is organized into a complex called the respirasome (Chapter 20)
• An isozymic form of glycogen phosphorylase exists in the brain (Chapter 24)
• AMP-activated protein kinase is a key regulator of metabolism (Chapter 28)
• Protein metabolism helps to power the flight of migratory birds (Chapter 30)
• Gene disruption and genome editing provide clues to gene function and opportunities for new therapies (Chapter 41).

Table of Contents

1. Part I The Molecular Design of Life 
   SECTION 1 Biochemistry Helps Us to Understand Our World
   Chapter 1 Biochemistry and the Unity of Life
   1.1 Living Systems Require a Limited Variety of Atoms and Molecules
   1.2 There Are Four Major Classes of Biomolecules
   Proteins Are Highly Versatile Biomolecules
   Nucleic Acids Are the Information Molecules of the Cell
   Lipids Are a Storage Form of Fuel and Serve as a Barrier
   Carbohydrates Are Fuels and Informational Molecules
   1.3 The Central Dogma Describes the Basic Principles of Biological Information Transfer
   1.4 Membranes Define the Cell and Carry Out Cellular Functions
   Biochemical Functions Are Sequestered in Cellular Compartments
   Some Organelles Process and Sort Proteins and Exchange Material with the Environment
   Clinical Insight Defects in Organelle Function May Lead to Disease
2. Chapter 2 Water, Weak Bonds, and the Generation of Order Out of Chaos
   2.1 Thermal Motions Power Biological Interactions
   2.2 Biochemical Interactions Take Place in an Aqueous Solution
   2.3 Weak Interactions Are Important Biochemical Properties
   Electrostatic Interactions Are Between Electrical Charges
   Hydrogen Bonds Form Between an Electronegative Atom and Hydrogen
   van der Waals Interactions Depend on Transient Asymmetry in Electrical Charge
   Weak Bonds Permit Repeated Interactions
   2.4 Hydrophobic Molecules Cluster Together
   Membrane Formation Is Powered by the Hydrophobic Effect
   Protein Folding Is Powered by the Hydrophobic Effect
   Functional Groups Have Specific Chemical Properties
   2.5 pH Is an Important Parameter of Biochemical Systems
   Water Ionizes to a Small Extent
   An Acid Is a Proton Donor, Whereas a Base Is a Proton Acceptor
   Acids Have Differing Tendencies to Ionize
   Buffers Resist Changes in pH
   Buffers Are Crucial in Biological Systems
   Making Buffers Is a Common Laboratory Practice
   APPENDIX: Problem-Solving Strategies
3. SECTION 2 Protein Composition and Structure
   Chapter 3 Amino Acids
   3.1 Proteins Are Built from a Repertoire of 20 Amino Acids
   Most Amino Acids Exist in Two Mirror-Image Forms
   All Amino Acids Have at Least Two Charged Groups
   3.2 Amino Acids Contain a Wide Array of Functional Groups
   Hydrophobic Amino Acids Have Mainly Hydrocarbon Side Chains
   Polar Amino Acids Have Side Chains That Contain an Electronegative Atom
   Positively Charged Amino Acids Are Hydrophilic
   Negatively Charged Amino Acids Have Acidic Side Chains
   The Ionizable Side Chains Enhance Reactivity and Bonding
   3.3 Essential Amino Acids Must Be Obtained from the Diet
   Clinical Insight Pathological Conditions Result If Protein Intake Is Inadequate
   APPENDIX: Problem-Solving Strategies
4. Chapter 4 Protein Three-Dimensional Structure
   4.1 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
   4.2 Secondary Structure: Polypeptide Chains Can Fold into Regular Structures
   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
   Fibrous Proteins Provide Structural Support for Cells and Tissues
   Clinical Insight Defects in Collagen Structure Result in Pathological Conditions
   4.3 Tertiary Structure: Water-Soluble Proteins Fold into Compact Structures
   Myoglobin Illustrates the Principles of Tertiary Structure
   The Tertiary Structure of Many Proteins Can Be Divided into Structural and Functional Units
   4.4 Quaternary Structure: Multiple Polypeptide Chains Can Assemble into a Single Protein
   4.5 The Amino Acid Sequence of a Protein Determines Its Three-Dimensional Structure
   Proteins Fold by the Progressive Stabilization of Intermediates Rather Than by Random Search
   Some Proteins Are Intrinsically Unstructured and Can Exist in Multiple Conformations
   Clinical Insight Protein Misfolding and Aggregation Are Associated with Some  Neurological Diseases
   APPENDIX: Biochemistry in Focus: Surviving desiccation
5. Chapter 5 Techniques in Protein Biochemistry
   5.1 The Proteome Is the Functional Representation of the Genome
   5.2 The Purification of a Protein Is the First Step in Understanding Its Function
   Proteins Can Be Purified on the Basis of Differences in

Author Biography

John L. Tymoczko is Towsley Professor of Biology at Carleton College, where he has taught since 1976. He currently teaches Biochemistry, the Metabolic Basisof Human Disease, Oncogenes and the Molecular Biology of Cancer, and Exercise Biochemistry and co-teaches an introductory course, Energy Flow in BiologicalSystems. Professor Tymoczko received his B.A. from the University in Chicago in 1970 and his Ph.D. in Biochemistry from the University of Chicago withShutsung Liao at the Ben May Institute for Cancer Research in 1973. He then held a postdoctoral position with Hewson Swift of the Department of Biology atthe University of Chicago. The focus of his research has been on steroid receptors, ribonucleoprotein particles, and proteolytic processing enzymes.