Test Bank Biochemistry A Short Course 4th Edition by John Tymoczko
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Test Bank Biochemistry A Short Course 4th Edition by John Tymoczko
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Test Bank Biochemistry A Short Course 4th Edition by John Tymoczko
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.
ISBN-10 1319114636
ISBN-13 : 978-1319114633
John L. Tymoczko (Author), Jeremy M. Berg (Author), Gregory J. Gatto Jr. (Author), Lubert Stryer (Author)
Table of Contents
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
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
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
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
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 Their Chemical Properties
Proteins Must Be Removed 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 Purification Scheme Can Be Quantitatively Evaluated
5.3 Immunological Techniques Are Used to Purify and Characterize Proteins
Centrifugation Is a Means of Separating Proteins
Gradient Centrifugation Provides an Assay for the Estradiol–Receptor Complex
Antibodies to Specific Proteins Can Be Generated
Monoclonal Antibodies with Virtually Any Desired Specificity Can Be Readily Prepared
The Estrogen Receptor Can Be Purified by Immunoprecipitation
Proteins Can Be Detected and Quantified with the Use of an Enzyme-Linked Immunosorbent Assay
Western Blotting Permits the Detection of Proteins Separated by Gel Electrophoresis
5.4 Determination of Primary Structure Facilitates an Understanding of Protein Function
Mass Spectrometry Can Be Used to Determine a Protein’s Mass, Identity, and Sequence
Amino Acids Are Sources of Many Kinds of Insight
APPENDIX: Biochemistry in Focus: The development of affinity chromatography
APPENDIX: Problem-Solving Strategies
SECTION 3 Basic Concepts and Kinetics of Enzymes
Chapter 6 Basic Concepts of Enzyme Action
6.1 Enzymes Are Powerful and Highly Specific Catalysts
Proteolytic Enzymes Illustrate the Range of Enzyme Specificity
There Are Six Major Classes of Enzymes
6.2 Many Enzymes Require Cofactors for Activity
6.3 Gibbs Free Energy Is a Useful Thermodynamic Function for Understanding Enzymes
The Free-Energy Change Provides Information About the Spontaneity but Not the Rate of a Reaction
The Standard Free-Energy Change of a Reaction Is Related to the Equilibrium Constant
Enzymes Alter the Reaction Rate but Not the Reaction Equilibrium
6.4 Enzymes Facilitate the Formation of the Transition State
The Formation of an Enzyme–Substrate Complex Is the First Step in Enzymatic Catalysis
The Active Sites of Enzymes Have Some Common Features
The Binding Energy Between Enzyme and Substrate Is Important for Catalysis
Transition-State Analogs Are Potent Inhibitors of Enzymes
APPENDIX: Biochemistry in Focus: Catalytic antibodies demonstrated the importance of selective binding of the transition state to enzymatic activity.
APPENDIX: Problem-Solving Strategies
Chapter 7 Kinetics and Regulation
7.1 Kinetics Is the Study of Reaction Rates
7.2 The Michaelis–Menten Model Describes the Kinetics of Many Enzymes
Clinical Insight Variations in KM Can Have Physiological Consequences
KM and Vmax Values Can Be Determined by Several Means
KM and Vmax Values Are Important Enzyme Characteristics
Kcat/KM Is a Measure of Catalytic Efficiency
Most Biochemical Reactions Include Multiple Substrates
7.3 Allosteric Enzymes Are Catalysts and Information Sensors
Allosteric Enzymes Are Regulated by Products of the Pathways Under Their Control
Allosterically Regulated Enzymes Do Not Conform to Michaelis–Menten Kinetics
Allosteric Enzymes Depend on Alterations in Quaternary Structure
Regulator Molecules Modulate the R
The Sequential Model Also Can Account for Allosteric Effects
Clinical Insight Loss of Allosteric Control May Re