biochemistry textbook stryer

Use Promo Code SHIPFREE at Step 4 of checkout. For several generations of students and teachers, Biochemistry has been an invaluable resource, presenting the concepts and details of molecular structure, metabolism, and laboratory techniques in a streamlined and engaging way. Applicants must propose one or more milestones for each Specific Aim. In this edition, as in all previous editions, the authors thoroughly revised the text with an eye for clarity, rewriting and reorganizing discussions where advances in the field have given us a different perspective on biochemistry. Digital innovation and trusted authorship transform the way biochemistry students learn. National Book Award; Newbery Medal; Nobel Prize for Literature; The Pulitzer Prize ; Hugo & Nebula Awards; Eisner Award; Packaging Option. Numerous examples and photos of biochemistry in action show students that biochemistry is part of everything they do and experience. This book is significantly detailed, but it is the go-to-the-point textbook for biochemistry. Read, highlight, and take notes, across web, tablet, and phone. You will need to find your course in order to purchase Achieve. It was initially written by Lubert Stryer and published by W. H. Freeman in 1975. You might not require more become old to spend to go to the book establishment as skillfully as search for them. Frustration-Free Packaging; International Shipping. Part I THE MOLECULAR DESIGN OF LIFEChapter 1 Biochemistry: An Evolving Science1.1 Biochemical Unity Underlies Biological Diversity 1.2 DNA Illustrates the Interplay Between Form and Function DNA is constructed from four building blocks Two single strands of DNA combine to form a double helix DNA structure explains heredity and the storage of information 1.3 Concepts from Chemistry Explain the Properties of Biological Molecules The formation of the DNA double helix as a key example The double helix can form from its component strands Covalent and noncovalent bonds are important for the structure and stability of biological molecules The double helix is an expression of the rules of chemistry The laws of thermodynamics govern the behavior of biochemical systems Heat is released in the formation of the double helix Acid–base reactions are central in many biochemical processes Acid–base reactions can disrupt the double helixBuffers regulate pH in organisms and in the laboratory 1.4 The Genomic Revolution Is Transforming Biochemistry, Medicine, and Other FieldsGenome sequencing has transformed biochemistry and other fields Environmental factors influence human biochemistry Genome sequences encode proteins and patterns of expression APPENDIX  Visualizing Molecular Structures: Small MoleculesAPPENDIX  Functional Groups, Chapter 2 Protein Composition and Structure2.1 Proteins Are Built from a Repertoire of 20 Amino Acids2.2 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 2.3 Secondary Structure: Polypeptide Chains Can Fold into Regular Structures Such As the Alpha Helix, the Beta Sheet, and Turns and Loops 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 2.4 Tertiary Structure: Proteins Can Fold into Globular or Fibrous Structures Fibrous proteins provide structural support for cells and tissues2.5 Quaternary Structure: Polypeptide Chains Can Assemble into Multisubunit Structures 2.6 The Amino Acid Sequence of a Protein Determines Its Three-Dimensional StructureAmino acids have different propensities for forming 〈 helices, ® sheets, and turns Protein folding is a highly cooperative process Proteins fold by progressive stabilization of intermediates rather than by random search Prediction of three-dimensional structure from sequence remains a great challenge Some proteins are inherently unstructured and can exist in multiple conformationsProtein misfolding and aggregation are associated with some neurological diseasesPosttranslational modifications confer new capabilities to proteins APPENDIX  Visualizing Molecular Structures: Proteins, Chapter 3 Exploring Proteins and Proteomes3.1 The Purification of Proteins Is an Essential First Step in Understanding Their Function The assay: How do we recognize the protein that we are looking for? Its straightforward and logical organization enhances clarity by stepping the reader through processes and helping them navigate complex pathways and mechanisms. Proteins must be released 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 protein purification scheme can be quantitatively evaluated Ultracentrifugation is valuable for separating biomolecules and determining their masses Protein purification can be made easier with the use of recombinant DNA technology 3.2 Immunology Provides Important Techniques with Which to Investigate ProteinsAntibodies to specific proteins can be generated Monoclonal antibodies with virtually any desired specificity can be readily prepared Proteins can be detected and quantified by using an enzyme-linked immunosorbent assay Western blotting permits the detection of proteins separated by gel electrophoresisCo-immunoprecipitation enables the identification of binding partners of a protein Fluorescent markers make the visualization of proteins in the cell possible 3.3 Mass Spectrometry Is a Powerful Technique for the Identification of Peptides and Proteins Peptides can be sequenced by mass spectrometry Proteins can be specifically cleaved into small peptides to facilitate analysisGenomic and proteomic methods are complementary The amino acid sequence of a protein provides valuable information Individual proteins can be identified by mass spectrometry 3.4 Peptides Can Be Synthesized by Automated Solid-Phase Methods 3.5 Three-Dimensional Protein Structure Can Be Determined by X-ray Crystallography, NMR Spectroscopy, and Cryo-Electron Microscopy X-ray crystallography reveals three-dimensional structure in atomic detail Nuclear magnetic resonance spectroscopy can reveal the structures of proteins in solution   Cryo-electron microscopy is an emerging method of protein structure determinationAPPENDIX  Problem-Solving Strategies, Chapter 4 DNA, RNA, and the Flow of Genetic Information4.1 A Nucleic Acid Consists of Four Kinds of Bases Linked to a Sugar–Phosphate Backbone RNA and DNA differ in the sugar component and one of the bases Nucleotides are the monomeric units of nucleic acids DNA molecules are very long and have directionality 4.2 A Pair of Nucleic Acid Strands with Complementary Sequences Can Form a Double-Helical Structure The double helix is stabilized by hydrogen bonds and van der Waals interactions DNA can assume a variety of structural forms  Some DNA molecules are circular and supercoiled Single-stranded nucleic acids can adopt elaborate structures 4.3 The Double Helix Facilitates the Accurate Transmission of Hereditary Information Differences in DNA density established the validity of the semiconservative replication hypothesis The double helix can be reversibly meltedUnusual circular DNA exists in the eukaryotic nucleus 4.4 DNA Is Replicated by Polymerases That Take Instructions from Templates DNA polymerase catalyzes phosphodiester-bridge formation The genes of some viruses are made of RNA 4.5 Gene Expression Is the Transformation of DNA Information into Functional Molecules Several kinds of RNA play key roles in gene expression All cellular RNA is synthesized by RNA polymerases RNA polymerases take instructions from DNA templates Transcription begins near promoter sites and ends at terminator sites Transfer RNAs are the adaptor molecules in protein synthesis 4.6 Amino Acids Are Encoded by Groups of Three Bases Starting from a Fixed Point Major features of the genetic code Messenger RNA contains start and stop signals for protein synthesis The genetic code is nearly universal 4.7 Most Eukaryotic Genes Are Mosaics of Introns and Exons RNA processing generates mature RNA Many exons encode protein domainsAPPENDIX  Problem-Solving Strategies Chapter 5 Exploring Genes and Genomes 5.1 The Exploration of Genes Relies on Key ToolsRestriction enzymes split DNA into specific fragments Restriction fragments can be separated by gel electrophoresis and visualized DNA can be sequenced by controlled termination of replication DNA probes and genes can be synthesized by automated solid-phase methods Selected DNA sequences can be greatly amplified by the polymerase chain reaction PCR is a powerful technique in medical diagnostics, forensics, and studies of molecular evolution The tools for recombinant DNA technology have been used to identify disease-causing mutations 5.2 Recombinant DNA Technology Has Revolutionized All Aspects of Biology Restriction enzymes and DNA ligase are key tools in forming recombinant DNA molecules Plasmids and ⎣ phage are choice vectors for DNA cloning in bacteria Bacterial and yeast artificial chromosomes Specific genes can be cloned from digests of genomic DNA Complementary DNA prepared from mRNA can be expressed in host cells Proteins with new functions can be created through directed changes in DNA Recombinant methods enable the exploration of the functional effects of disease-causing mutations 5.3 Complete Genomes Have Been Sequenced and Analyzed The genomes of organisms ranging from bacteria to multicellular eukaryotes have been sequenced The sequence of the human genome has been completed Next-generation sequencing methods enable the rapid determination of a complete genome sequence Comparative genomics has become a powerful research tool 5.4 Eukaryotic Genes Can Be Quantitated and Manipulated with Considerable Precision Gene-expression levels can be comprehensively examined New genes inserted into eukaryotic cells can be efficiently expressed Transgenic animals harbor and express genes introduced into their germ lines Gene disruption and genome editing provide clues to gene function and opportunities for new therapies RNA interference provides an additional tool for disrupting gene expression Tumor-inducing plasmids can be used to introduce new genes into plant cells Human gene therapy holds great promise for medicineAPPENDIX  Biochemistry in Focus: Improved biofuel production from genetically-engineered algae Chapter 6 Exploring Evolution and Bioinformatics 6.1 Homologs Are Descended from a Common Ancestor 6.2 Statistical Analysis of Sequence Alignments Can Detect Homology The statistical significance of alignments can be estimated by shuffling Distant evolutionary relationships can be detected through the use of substitution matrices Databases can be searched to identify homologous sequences 6.3 Examination of Three-Dimensional Structure Enhances Our Understanding of Evolutionary Relationships Tertiary structure is more conserved than primary structure Knowledge of three-dimensional structures can aid in the evaluation of sequence alignments Repeated motifs can be detected by aligning sequences with themselves Convergent evolution illustrates common solutions to biochemical challenges Comparison of RNA sequences can be a source of insight into RNA secondary structures 6.4 Evolutionary Trees Can Be Constructed on the Basis of Sequence Information Horizontal gene transfer events may explain unexpected branches of the evolutionary tree 6.5 Modern Techniques Make the Experimental Exploration of Evolution Possible Ancient DNA can sometimes be amplified and sequenced Molecular evolution can be examined experimentallyAPPENDIX  Biochemistry in Focus: Using sequence alignments to identify functionally important residuesAPPENDIX  Problem-Solving Strategies Chapter 7 Hemoglobin: Portrait of a Protein in Action7.1  Binding of Oxygen by Heme IronChanges in heme electronic structure upon oxygen binding are the basis for functional imaging studies The structure of myoglobin prevents the release of reactive oxygen species Human hemoglobin is an assembly of four myoglobin-like subunits 7.2 Hemoglobin Binds Oxygen Cooperatively Oxygen binding markedly changes the quaternary structure of hemoglobin Hemoglobin cooperativity can be potentially explained by several models Structural changes at the heme groups are transmitted to the 〈1®1–〈2®2 interface 2,3-Bisphosphoglycerate in red cells is crucial in determining the oxygen affinity of hemoglobin Carbon monoxide can disrupt oxygen transport by hemoglobin 7.3 Hydrogen Ions and Carbon Dioxide Promote the Release of Oxygen: The Bohr Effect 7.4 Mutations in Genes Encoding Hemoglobin Subunits Can Result in Disease Sickle-cell anemia results from the aggregation of mutated deoxyhemoglobin molecules Thalassemia is caused by an imbalanced production of hemoglobin chains The accumulation of free alpha-hemoglobin chains is prevented Additional globins are encoded in the human genome APPENDIX  Binding Models Can Be Formulated in Quantitative Terms: The Hill Plot and the Concerted ModelAPPENDIX  Biochemistry in Focus: A potential antidote for carbon monoxide poisoning? 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