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cover image - Principles of Medical Biochemistry,4th Edition
ISBN: 9780323296168
Publication Date: 11-28-2016
Page Count: 657
Imprint: Elsevier
List Price: $77.99

Principles of Medical Biochemistry, 4th Edition

by Gerhard Meisenberg, PhD and William H. Simmons, PhD


cover image - Principles of Medical Biochemistry,4th Edition
ISBN: 9780323296168
Publication Date: 11-28-2016
Page Count: 657
Imprint: Elsevier
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    • Just the right amount of detail on biochemistry, cell biology, and genetics – in one easy-to-digest textbook.
    • Full-color illustrations and tables throughout help students master challenging concepts more easily.
    • Online case studies serve as a self-assessment and review tool before exams.
    • Glossary of technical terms, both in print and online.
    • Clinical Boxes and Clinical Content demonstrate the integration of basic sciences and clinical applications, helping readers make connections between the two. New clinical examples have been added throughout the text.
    • Student Consult eBook version included with purchase. This enhanced eBook experience includes access -- on a variety of devices -- to the complete text, images, and references from the book.
  • Part ONE



    Chapter 1


    Water Is the Solvent of Life

    Water Contains Hydronium Ions and Hydroxyl Ions

    Ionizable Groups Are Characterized by Their pK Values

    The Blood pH is Tightly Regulated

    Acidosis and Alkalosis Are Common in Clinical Practice

    Bonds Are Formed by Reactions between Functional Groups

    Isomeric Forms Are Common in Biomolecules

    Properties of Biomolecules Are Determined by Their Noncovalent


    Triglycerides Consist of Fatty Acids and Glycerol

    Monosaccharides Are Polyalcohols with a Keto Group or an

    Aldehyde Group

    Monosaccharides Form Ring Structures

    Complex Carbohydrates Are Formed by Glycosidic Bonds

    Polypeptides Are Formed from Amino Acids

    Nucleic Acids Are Formed from Nucleotides

    Most Biomolecules Are Polymers


    Chapter 2


    Amino Acids Are Zwitterions

    Amino Acid Side Chains Form Many Noncovalent


    Peptide Bonds and Disulfide Bonds Form the Primary Structure of


    Proteins Can Fold Themselves into Many Shapes

    a-Helix and ß-Pleated Sheet Are the Most Common Secondary

    Structures in Proteins

    Globular Proteins Have a Hydrophobic Core

    Proteins Lose Their Biological Activities When Their Higher-Order

    Structure Is Destroyed

    The Solubility of Proteins Depends on pH and Salt


    Proteins Absorb Ultraviolet Radiation

    Proteins Can Be Separated by Their Charge or Their Molecular


    Abnormal Protein Aggregates Can Cause Disease

    Neurodegenerative Diseases Are Caused by Protein Aggregates

    Protein Misfolding Can Be Contagious


    Chapter 3



    The Heme Group Is the Oxygen-Binding Site of Hemoglobin and


    Myoglobin Is a Tightly Packed Globular Protein

    Red Blood Cells Are Specialized for Oxygen Transport

    The Hemoglobins Are Tetrameric Proteins

    Oxygenated and Deoxygenated Hemoglobin Have Different

    Quaternary Structures

    Oxygen Binding to Hemoglobin Is Cooperative

    2,3-Bisphosphoglycerate Is a Negative Allosteric Effector of

    Oxygen Binding to Hemoglobin

    Fetal Hemoglobin Has a Higher Oxygen-Binding Affinity than

    Does Adult Hemoglobin

    The Bohr Effect Facilitates Oxygen Delivery

    Most Carbon Dioxide Is Transported as Bicarbonate

    Summary 38

    Chapter 4


    The Equilibrium Constant Describes the Equilibrium of the


    The Free Energy Change Is the Driving Force for Chemical


    The Standard Free Energy Change Determines the Equilibrium

    Enzymes Are Both Powerful and Selective

    The Substrate Must Bind to Its Enzyme before the Reaction Can


    Rate Constants Are Useful for Describing Reaction Rates

    Enzymes Decrease the Free Energy of Activation

    Many Enzymatic Reactions Can Be Described by Michaelis-Menten


    Km and Vmax Can Be Determined Graphically

    Substrate Half-Life Can Be Determined for First-Order but Not

    Zero-Order Reactions

    Kcat/Km Predicts the Enzyme Activity at Low Substrate


    Allosteric Enzymes Do Not Conform to Michaelis-Menten


    Enzyme Activity Depends on Temperature and pH

    Different Types of Reversible Enzyme Inhibition Can Be

    Distinguished Kinetically

    Enzymes Stabilize the Transition State

    Chymotrypsin Forms a Transient Covalent Bond during



    Chapter 5


    Enzymes Are Classified According to Their Reaction Type

    Adenosine Triphosphate Has Two Energy-Rich Bonds

    ATP Is the Phosphate Donor in Phosphorylation Reactions

    ATP Hydrolysis Drives Endergonic Reactions

    Cells Always Try to Maintain a High Energy Charge

    Dehydrogenase Reactions Require Specialized Coenzymes

    Coenzyme A Activates Organic Acids

    S-Adenosyl Methionine Donates Methyl Groups

    Many Enzymes Require a Metal Ion


    Part TWO



    Chapter 6


    All Living Organisms Use DNA as Their Genetic Databank

    DNA Contains Four Bases

    DNA Forms a Double Helix

    DNA Can Be Denatured

    DNA Is Supercoiled

    DNA Replication Is Semiconservative

    DNA Is Synthesized by DNA Polymerases

    DNA Polymerases Have Exonuclease Activities

    Unwinding Proteins Present a Single-Stranded Template to the

    DNA Polymerases

    One of the New DNA Strands Is Synthesized Discontinuously

    RNA Plays Key Roles in Gene Expression

    The S Subunit Recognizes Promoters

    DNA Is Faithfully Copied into RNA

    Some RNAs Are Chemically Modified after Transcription

    The Genetic Code Defines the Structural Relationship between mRNA and Polypeptide

    Transfer RNA Is the Adapter Molecule in Protein Synthesis

    Amino Acids Are Activated by an Ester Bond with the 3' Terminus

    of the tRNA

    Many Transfer RNAs Recognize More than One Codon

    Ribosomes Are the Workbenches for Protein Synthesis

    The Initiation Complex Brings Together Ribosome, Messenger

    RNA, and Initiator tRNA

    Polypeptides Grow Stepwise from the Amino Terminus to the

    Carboxyl Terminus

    Protein Synthesis Is Energetically Expensive

    Gene Expression Is Tightly Regulated

    A Repressor Protein Regulates Transcription of the lac Operon

    in E. coli

    Anabolic Operons Are Repressed by the End Product of the


    Glucose Regulates the Transcription of Many Catabolic


    Transcriptional Regulation Depends on DNA-Binding

  • Gerhard Meisenberg, PhD, Course Director Medical Biochemistry, Ross University, Dominica, West Indies and William H. Simmons, PhD, Department of Molecular Pharmacology and Therapeutics, Loyola University School of Medicine, Maywood, Illinois
In Stock
Most review copies are eBooks – how fast!
A review copy request is most likely to be fulfilled as an eBook on VitalSource rather than a print product, unless no eBook is available. eBooks become available in as little as a few hours. Print products will take between 7 and 10 days to arrive. To request a print copy, please contact the Evolve Support Center or your Education Solutions Consultant.
Important note
This is a Faculty Product!
Any student who attempts to request a review copy will be reported to the school's faculty and administration.