عنوان

Essential biochemistry /

111933747X

9781119337478

1119012376

9781119012375

Essential biochemistry /

[Book]

Charlotte W. Pratt, Kathleen Cornely.

Fourth edition.

Hoboken, NJ :

Wiley,

[2018]

1 online resource (726 pages)

Includes bibliographical references and index.

Cover -- Title Page -- Copyright -- About the Authors -- Brief Contents -- Contents -- Preface -- Acknowledgments -- Part 1 Foundations -- 1 The Chemical Basis of Life -- 1.1 What Is Biochemistry? -- 1.2 Biological Molecules -- Cells contain four major types of biomolecules -- There are three major kinds of biological polymers -- Box 1.A Units Used in Biochemistry -- 1.3 Energy and Metabolism -- Enthalpy and entropy are components of free energy -- Î#x94;G is less than zero for a spontaneous process -- Life is thermodynamically possible -- 1.4 The Origin and Evolution of Life -- The prebiotic world -- Origins of modern cells -- Box 1.B How Does Evolution Work? -- 2 Aqueous Chemistry -- 2.1 Water Molecules and Hydrogen Bonds -- Hydrogen bonds are one type of electrostatic force -- Box 2.A Why Do Some Drugs Contain Fluorine? -- Water dissolves many compounds -- 2.2 The Hydrophobic Effect -- Amphiphilic molecules experience both hydrophilic interactions and the hydrophobic effect -- The hydrophobic core of a lipid bilayer is a barrier to diff usion -- Box 2.B Sweat, Exercise, and Sports Drinks -- 2.3 Acid-Base Chemistry -- [H+] and [OH-] are inversely related -- The pH of a solution can be altered -- Box 2.C Atmospheric CO2 and Ocean Acidification -- A pK value describes an acid's tendency to ionize -- The pH of a solution of acid is related to the pK -- 2.4 Tools and Techniques: Buffers -- 2.5 Clinical Connection: Acid-Base Balance in Humans -- Part 2 Molecular Structure and Function -- 3 From Genes to Proteins -- 3.1 Nucleotides -- Nucleic acids are polymers of nucleotides -- Some nucleotides have other functions -- 3.2 Nucleic Acid Structure -- DNA is a double helix -- RNA is single-stranded -- Nucleic acids can be denatured and renatured -- 3.3 The Central Dogma -- DNA must be decoded -- A mutated gene can cause disease -- 3.4 Genomics.

7.1 Introduction to Enzyme Kinetics -- 7.2 Derivation and Meaning of the Michaelis-Menten Equation -- Rate equations describe chemical processes -- The Michaelis-Menten equation is a rate equation for an enzyme-catalyzed reaction -- KM is the substrate concentration at which velocity is half-maximal -- The catalytic constant describes how quickly an enzyme can act -- kcat/KM indicates catalytic efficiency -- KM and Vmax are experimentally determined -- Not all enzymes fit the simple Michaelis-Menten model -- 7.3 Enzyme Inhibition -- Some inhibitors act irreversibly -- Competitive inhibition is the most common form of reversible enzyme inhibition -- Transition state analogs inhibit enzymes -- Box 7.A Inhibitors of HIV Protease -- Other types of inhibitors aff ect Vmax -- Allosteric enzyme regulation includes inhibition and activation -- Several factors may influence enzyme activity -- 7.4 Clinical Connection: Drug Development -- 8 Lipids and Membranes -- 8.1 Lipids -- Fatty acids contain long hydrocarbon chains -- Box 8.A Omega-3 Fatty Acids -- Some lipids contain polar head groups -- Lipids perform a variety of physiological functions -- Box 8.B The Lipid Vitamins A, D, E, and K -- 8.2 The Lipid Bilayer -- The bilayer is a fluid structure -- Natural bilayers are asymmetric -- 8.3 Membrane Proteins -- Integral membrane proteins span the bilayer -- An a helix can cross the bilayer -- A transmembrane Ã#x9F; sheet forms a barrel -- Lipid-linked proteins are anchored in the membrane -- 8.4 The Fluid Mosaic Model -- Membrane glycoproteins face the cell exterior -- 9 Membrane Transport -- 9.1 The Thermodynamics of Membrane Transport -- Ion movements alter membrane potential -- Membrane proteins mediate transmembrane ion movement -- 9.2 Passive Transport -- Porins are Ã#x9F; barrel proteins -- Ion channels are highly selective -- Box 9.A Pores Can Kill.

Gated channels undergo conformational changes -- Aquaporins are water-specific pores -- Some transport proteins alternate between conformations -- 9.3 Active Transport -- The Na, K-ATPase changes conformation as it pumps ions across the membrane -- ABC transporters mediate drug resistance -- Secondary active transport exploits existing gradients -- 9.4 Membrane Fusion -- Box 9.B Antidepressants Block Serotonin Transport -- SNAREs link vesicle and plasma membranes -- Endocytosis is the reverse of exocytosis -- Box 9.C Exosomes -- 10 Signaling -- 10.1 General Features of Signaling Pathways -- A ligand binds to a receptor with a characteristic affinity -- Box 10.A Bacterial Quorum Sensing -- Most signaling occurs through two types of receptors -- The effects of signaling are limited -- 10.2 G Protein Signaling Pathways -- G protein-coupled receptors include seven transmembrane helices -- The receptor activates a G protein -- Adenylate cyclase generates the second messenger cyclic AMP -- Cyclic AMP activates protein kinase A -- Signaling pathways are also switched off -- The phosphoinositide signaling pathway generates two second messengers -- Calmodulin mediates some Ca2+ signals -- 10.3 Receptor Tyrosine Kinases -- The insulin receptor dimer binds one insulin -- The receptor undergoes autophosphorylation -- Box 10.B Cell Signaling and Cancer -- 10.4 Lipid Hormone Signaling -- Eicosanoids are short-range signals -- Box 10.C Aspirin and Other Inhibitors of Cyclooxygenase -- 11 Carbohydrates -- 11.1 Monosaccharides -- Most carbohydrates are chiral compounds -- Cyclization generates a and Ã#x9F; anomers -- Monosaccharides can be derivatized in many different ways -- 11.2 Polysaccharides -- Lactose and sucrose are the most common disaccharides -- Starch and glycogen are fuel-storage molecules -- Cellulose and chitin provide structural support.

Gene number is roughly correlated with organismal complexity -- Genes are identified by comparing sequences -- Genomic data reveal biological functions -- 3.5 Tools and Techniques: Manipulating DNA -- Cutting and pasting generates recombinant DNA -- The polymerase chain reaction amplifies DNA -- Box 3.A Genetically Modified Organisms -- Box 3.B DNA Fingerprinting -- DNA sequencing uses DNA polymerase to make a complementary strand -- DNA can be altered -- 4 Protein Structure -- 4.1 Amino Acids, the Building Blocks of Proteins -- The 20 amino acids have different chemical properties -- Box 4.A Does Chirality Matter? -- Box 4.B Monosodium Glutamate -- Peptide bonds link amino acids in proteins -- The amino acid sequence is the first level of protein structure -- 4.2 Secondary Structure: The Conformation of the Peptide Group -- The a helix exhibits a twisted backbone conformation -- The Ã#x9F; sheet contains multiple polypeptide strands -- Proteins also contain irregular secondary structure -- 4.3 Tertiary Structure and Protein Stability -- Proteins have hydrophobic cores -- Protein structures are stabilized mainly by the hydrophobic effect -- Other interactions help stabilize proteins -- Protein folding begins with the formation of secondary structures -- Some proteins have more than one conformation -- 4.4 Quaternary Structure -- 4.5 Clinical Connection: Protein Misfolding and Disease -- 4.6 Tools and Techniques: Analyzing Protein Structure -- Chromatography takes advantage of a polypeptide's unique properties -- Mass spectrometry reveals amino acid sequences -- Protein structures are determined by X-ray crystallography, electron crystallography, and NMR spectroscopy -- Box 4.C Mass Spectrometry Applications -- 5 Protein Function -- 5.1 Myoglobin and Hemoglobin: Oxygen-Binding Proteins -- Oxygen binding to myoglobin depends on the oxygen concentration.

Myoglobin and hemoglobin are related by evolution -- Oxygen binds cooperatively to hemoglobin -- A conformational shift explains hemoglobin's cooperative behavior -- Box 5.A Carbon Monoxide Poisoning -- H+ ions and bisphosphoglycerate regulate oxygen binding to hemoglobin in vivo -- 5.2 Clinical Connection: Hemoglobin Variants -- 5.3 Structural Proteins -- Actin filaments are most abundant -- Actin filaments continuously extend and retract -- Tubulin forms hollow microtubules -- Some drugs aff ect microtubules -- Keratin is an intermediate filament -- Collagen is a triple helix -- Box 5.B Vitamin C Deficiency Causes Scurvy -- Collagen molecules are covalently cross-linked -- Box 5.C Bone and Collagen Defects -- 5.4 Motor Proteins -- Myosin has two heads and a long tail -- Myosin operates through a lever mechanism -- Kinesin is a microtubule-associated motor protein -- Box 5.D Myosin Mutations and Deafness -- Kinesin is a processive motor -- 6 How Enzymes Work -- 6.1 What Is an Enzyme? -- Enzymes are usually named after the reaction they catalyze -- 6.2 Chemical Catalytic Mechanisms -- A catalyst provides a reaction pathway with a lower activation energy barrier -- Enzymes use chemical catalytic mechanisms -- Box 6.A Depicting Reaction Mechanisms -- The catalytic triad of chymotrypsin promotes peptide bond hydrolysis -- 6.3 Unique Properties of Enzyme Catalysts -- Enzymes stabilize the transition state -- Eff icient catalysis depends on proximity and orientation effects -- The active-site microenvironment promotes catalysis -- 6.4 Chymotrypsin in Context -- Not all serine proteases are related by evolution -- Enzymes with similar mechanisms exhibit different substrate specificity -- Chymotrypsin is activated by proteolysis -- Protease inhibitors limit protease activity -- 6.5 Clinical Connection: Blood Coagulation -- 7 Enzyme Kinetics and Inhibition.

0

8

8

8

8

Essential Biochemistry, 4th Edition.

9781119012375

Biochemistry.

Biochemistry.

SCIENCE-- Life Sciences-- Biochemistry.

SCI-- 007000

Pratt, Charlotte W.

Cornely, Kathleen.

20200822152153.0

pn

[Book]

Y