Gerhard Meisenberg, William H. Simmons

Principles of Medical Biochemistry E-Book (eBook, ePUB)

Principles of Medical Biochemistry E-Book

• Format: ePub

Produktbeschreibung

For nearly 30 years, Principles of Medical Biochemistry has integrated medical biochemistry with molecular genetics, cell biology, and genetics to provide complete yet concise coverage that links biochemistry with clinical medicine. The 4th Edition of this award-winning text by Drs. Gerhard Meisenberg and William H. Simmons has been fully updated with new clinical examples, expanded coverage of recent changes in the field, and many new case studies online. A highly visual format helps readers retain complex information, and USMLE-style questions (in print and online) assist with exam preparation.

• 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.
• Online access includes nearly 150 USMLE-style questions in addition to the questions that are in the book.
• Glossary of technical terms.

• 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.

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Produktdetails

• Verlag: Elsevier HealthScience EN
• Seitenzahl: 600
• Erscheinungstermin: 28. September 2016
• Englisch
• ISBN-13: 9780323391900
• Artikelnr.: 46753475

Autorenporträt

Dr. Meisenberg emailed us Jan. 24, 2019 to note his updated email address [e-mail] since he has now officially retired from his university position.

Inhaltsangabe

Part ONE

PRINCIPLES OF MOLECULAR STRUCTURE AND

FUNCTION 1

Chapter 1

INTRODUCTION TO BIOMOLECULES

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

Interactions

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

Summary

Chapter 2

INTRODUCTION TO PROTEIN STRUCTURE

Amino Acids Are Zwitterions

Amino Acid Side Chains Form Many Noncovalent

Interactions

Peptide Bonds and Disulfide Bonds Form the Primary Structure of

Proteins

Proteins Can Fold Themselves into Many Shapes

_-Helix and beta-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

Concentration

Proteins Absorb Ultraviolet Radiation

Proteins Can Be Separated by Their Charge or Their Molecular

Weight

Abnormal Protein Aggregates Can Cause Disease

Neurodegenerative Diseases Are Caused by Protein Aggregates

Protein Misfolding Can Be Contagious

Summary

Chapter 3

OXYGEN TRANSPORTERS: HEMOGLOBIN AND

MYOGLOBIN

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

Myoglobin

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

ENZYMATIC REACTIONS 39

The Equilibrium Constant Describes the Equilibrium of the

Reaction

The Free Energy Change Is the Driving Force for Chemical

Reactions

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

Proceed

Rate Constants Are Useful for Describing Reaction Rates

Enzymes Decrease the Free Energy of Activation

Many Enzymatic Reactions Can Be Described by Michaelis-Menten

Kinetics



K_m and V_max Can Be Determined Graphically

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

Zero-Order Reactions



K_cat/K_m Predicts the Enzyme Activity at Low Substrate

Concentration

Allosteric Enzymes Do Not Conform to Michaelis-Menten

Kinetics

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 dur