Biochemistry for Dummies - John T Moore

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Résumé :

Introduction?1

About This Book 1

Foolish Assumptions 2

Icons Used in This Book 3

Beyond the Book 3

Where to Go from Here 4

Part 1: Setting the Stage: Basic Biochemistry Concepts?5

Chapter 1: Biochemistry: What You Need to Know and Why?7

Why Biochemistry? 7

What Is Biochemistry and Where Does It Take Place? 8

Types of Living Cells 8

Prokaryotes 9

Eukaryotes 9

Animal Cells and How They Work 10

A Brief Look at Plant Cells 12

Chapter 2: Seems So Basic: Water Chemistry and pH?15

The Fundamentals of H2O 16

Let's get wet! The physical properties of water 16

Water's most important biochemical role: The solvent 18

Hydrogen Ion Concentration: Acids and Bases 20

Achieving equilibrium 20

Understanding the pH scale 21

Calculating pOH 23

Applying the Br?nsted-Lowry theory 23

Buffers and pH Control 27

Identifying common physiological buffers 27

Calculating a buffer's pH 28

Chapter 3: Fun with Carbon: Organic Chemistry?31

The Role of Carbon in the Study of Life 31

It's All in the Numbers: Carbon Bonds 33

When Forces Attract: Bond Strengths 33

Everybody has 'em: Intermolecular forces 34

Water-related interactions: Both the lovers and the haters 35

How bond strengths affect physical properties of substances 35

Getting a Reaction out of a Molecule: Functional Groups 37

Hydrocarbons 37

Functional groups with oxygen and sulfur 37

Functional groups containing nitrogen 38

Functional groups containing phosphorus 39

Reactions of functional groups 40

pH and functional groups 43

Same Content, Different Structure: Isomerism 44

Cis-trans isomers 44

Chiral carbons 44

Part 2: The Meat of Biochemistry: Proteins?47

Chapter 4: Amino Acids: The Building Blocks of Protein?49

General Properties of Amino Acids 50

Amino acids are positive and negative: The zwitterion formation 50

Protonated? pH and the isoelectric point 51

Asymmetry: Chiral amino acids 52

The Magic 20 Amino Acids 53

Nonpolar (hydrophobic) and uncharged amino acids 53

Polar (hydrophilic) and uncharged amino acids 55

Acidic amino acids 57

Basic amino acids 57

Lest We Forget: Rarer Amino Acids 58

Rudiments of Amino Acid Interactions 59

Intermolecular forces: How an amino acid interacts with other molecules 59

Altering interactions by changing the pH 61

Combining Amino Acids: How It Works 62

The peptide bond and the dipeptide 63

Tripeptide: Adding an amino acid to a dipeptide 64

Chapter 5: Protein Structure and Function?65

Proteins: Not Just for Dinner 65

Primary Structure: The Structure Level All Proteins Have 67

Building a protein: Outlining the process 67

Organizing the amino acids 68

Example: The primary structure of insulin 69

Secondary Structure: A Structure Level Most Proteins Have 69

The -helix 70

The -pleated sheet 71

-turns and the -loops 73

Tertiary Structure: A Structure Level Many Proteins Have 74

Quaternary Structure: A Structure Level Some Proteins Have 75

Dissecting a Protein for Study 75

Separating proteins within a cell and purifying them 75

Digging into the details: Uncovering a protein's amino acid sequence 78

Chapter 6: Enzyme Kinetics: Getting There Faster?83

Enzyme Classification: The Best Catalyst for the Job 84

Up one, down one: Oxid...

Biographie:

John T. Moore, EdD, and Richard H. Langley, PhD, teach Chemistry at Stephen F. Austin State University. Together they have more than 8.9 x 10¹ years of science education experience, and they have authored or coauthored oodles of books on chemistry topics.