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Dynamics in Enzyme Catalysis / / edited by Judith Klinman, Sharon Hammes- Schiffer
| Dynamics in Enzyme Catalysis / / edited by Judith Klinman, Sharon Hammes- Schiffer |
| Edizione | [1st ed. 2013.] |
| Pubbl/distr/stampa | Berlin, Heidelberg : , : Springer Berlin Heidelberg : , : Imprint : Springer, , 2013 |
| Descrizione fisica | 1 online resource (IX, 212 p.) |
| Disciplina | 572/.4 |
| Collana | Topics in Current Chemistry |
| Soggetto topico |
Catalysis
Proteins Chemistry, Physical and theoretical Protein Science Theoretical and Computational Chemistry |
| ISBN | 3-642-38962-7 |
| Formato | Materiale a stampa  |
| Livello bibliografico | Monografia |
| Lingua di pubblicazione | eng |
| Nota di contenuto | Relationship of Femtosecond–Picosecond Dynamics to Enzyme-Catalyzed H-Transfer -- Protein Conformational Disorder and Enzyme Catalysis -- A Surprising Role for Conformational Entropy in Protein Function -- Conformational Heterogeneity Within the LID Domain Mediates Substrate Binding to Escherichia coli Adenylate Kinase: Function Follows Fluctuations -- Structured Crowding and Its Effects on Enzyme Catalysis -- Allosteric Activation Transitions in Enzymes and Biomolecular Motors: Insights from Atomistic and Coarse-Grained Simulations -- Multiple Intermediates, Diverse Conformations, and Cooperative Conformational Changes Underlie the Catalytic Hydride Transfer Reaction of Dihydrofolate Reductase -- Protein Dynamics and the Enzymatic Reaction Coordinate. |
| Record Nr. | UNINA-9910437810203321 |
| Berlin, Heidelberg : , : Springer Berlin Heidelberg : , : Imprint : Springer, , 2013 | ||
| Materiale a stampa | ||
| Lo trovi qui: Univ. Federico II | ||
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Molecular Life Sciences : An Encyclopedic Reference / / edited by Robert D. Wells, Judith S. Bond, Judith Klinman, Bettie Sue Siler Masters, Ellis Bell, Laurie S. Kaguni
| Molecular Life Sciences : An Encyclopedic Reference / / edited by Robert D. Wells, Judith S. Bond, Judith Klinman, Bettie Sue Siler Masters, Ellis Bell, Laurie S. Kaguni |
| Edizione | [1st ed. 2018.] |
| Pubbl/distr/stampa | New York, NY : , : Springer New York : , : Imprint : Springer, , 2018 |
| Descrizione fisica | 1 online resource (456 illus., 307 illus. in color. eReference.) |
| Disciplina | 572 |
| Collana | Springer reference |
| Soggetto topico |
Biochemistry
Microbiology Biophysics Biological physics Biochemistry, general Biological and Medical Physics, Biophysics |
| ISBN |
1-78785-233-4
1-4614-1531-4 |
| Formato | Materiale a stampa |
| Livello bibliografico | Monografia |
| Lingua di pubblicazione | eng |
| Nota di contenuto | Allostery and Quaternary Structure -- Analysis of Damaged DNA -- Artificial Chromosomes -- Artificial Endonucleases for Genome Editing -- Bacterial DNA Replicases -- Bacteriophage and Viral Cloning Vectors -- Base Intercalation -- Bioactivation of Carcinogens -- Bioinorganic Chemistry -- Blue/White Selection -- Characteristics of Enzymes and Cloning Vectors Used to Create Recombinant DNA -- Chemical Biology of DNA Replication -- Chemical Denaturation -- Chemical Reaction Kinetics: Mathematical Underpinnings -- Chromatin Remodeling during Homologous Recombination Repair in Saccharomyces Cerevisiae -- Cis-Regulation of Eukaryotic Transcription -- Classic Approaches to sequence determination -- Classical and Alternative End Joining -- Cloning Vector Compatibility -- Computational methods in epigenetic research -- Conjugative Transfer Systems and Classifying Plasmid Genomes -- Conservative Site-specific Recombination -- Control of Initiation in E.coli -- Co-Transcriptional mRNA Processing in Eukaryotes -- Crosslinking -- Cycling of the Lagging Strand Replicase During Okazaki Fragment Synthesis -- Depurination -- Differential Equations and Chemical Master Equation Models for Gene Regulatory Networks -- Direct Enzymatic Reversal of DNA Damage -- Division of Labor -- DNA Damage as a Therapeutic Strategy -- DNA Damage by Endogenous Chemicals -- DNA Methylation and Cancer -- DNA Polymerase III Structure -- DNA Repair -- DNA Repair Polymerases -- DNA Replication -- DNA Topology and Topoisomerases -- DnaA, DnaB, DnaC -- DnaX Complex Composition and Assembly Within Cells -- Double-strand Break Repair -- Effects of adducts on Tm -- Equilibria and Bifurcations in the Molecular Biosciences -- Eukaryotic DNA Replicases -- Evolution of Gene Regulatory Networks -- Evolution of Plant Genomes -- Exocyclic Adducts -- Experimental Assessment of Secondary Structure by Circular Dichroism -- Exploring Nuclear Lamin–Chromatin Interactions and Their Signalling Cascades -- Expression Assessment -- Fatty Acid Metabolism -- Forces Maintaining the Stability of Tertiary Structure -- Frequency of DNA Damage -- Gene Regulation -- Genes and Genomes: Structure -- Genomic Imprinting -- Genomic Imprinting in Mammals: Memories of Generations Past -- Genomic Sequence and Structural Diversity in Plants -- Genomic Signature Analysis to Predict Plasmid Host Range -- Golgi Apparatus -- Gyrase and Topoisomerase IV as Targets for Antibacterial Drugs -- HDAC Inhibitors Entinostat and Suberoylanilide Hydroxamic Acid (SAHA): The Ray of Hope for Cancer Therapy -- Helicase and Primase Interactions with Replisome Components and Accessory Factors -- Helicase Mechanism of Action -- Hereditary Breast and Ovarian Cancer and Poly(ADP-ribose) Polymerase Inhibition -- Homologous Recombination in Lesion Bypass -- Hydrolytic, Deamination, and Rearrangement Reactions of DNA Adducts -- Immunology and the Immune Response -- In Silico Approaches Towards Safe Targetting of Class I Histone Deacetylases -- Inflammation and Host Response to Infection -- Innate and Regulatory B cells -- Innate Immunity -- Ion Channels and Transporters -- Kinetics of DNA Damage -- Large, Theta-replicating Plasmids -- Long-Term Genetic Silencing at Centromere and Telomeres -- Mammalian Sugar Transporters -- Many Bacteria Use a Special Mutagenic Pol III in Place of Pol V -- Mass Spectrometry Approaches -- Mathematical Modelling of Plasmid Dynamics -- Mathematical Models in the Sciences -- Mathematics of Fitting Scientific Data -- Mechanism of Initiation Complex Formation -- Mechanism of PCNA loading by RFC -- Mechanisms of DNA Recombination -- Meiotic Recombination -- Metamobilomics – The Plasmid Metagenome of Natural Environments -- Methods for Plant Genome Annotation -- Mismatch Repair -- Mitochondrial Genomes -- Mitochondrial Genomes in Alveolates -- Mitochondrial Genomes in Amoebozoa -- Mitochondrial Genomes in Fungi -- Mitochondrial Genomes in Invertebrate Animals -- Mitochondrial Genomes in Land Plants -- Mitochondrial Genomes in Unicellular Relatives of Animals -- Mitochondrial Genomes in Vertebrate Animals -- Mitochondrial Genomes of Chromists (Stramenopiles, Haptophytes and Cryptophytes) -- Mitochondrial Genomes of Excavata -- Mitochondrial Genomes of Green, Red and Glaucophyte Algae -- Mobile DNA: Mechanisms, Utility, and Consequences -- Modelling Plasmid Regulatory Systems -- Modes of Base Pairing -- mRNA localization and localized translation -- Naming and Annotation of plasmids -- Natural Products that Damage DNA -- NMR Approaches to Determine Protein Structure -- NMR Basis For Biomolecular Structure (Theory) -- Nucleotide Excision Repair -- Obtaining Crystals -- Oxidative Damage -- Pattern Recognition Receptors: Evolution, Redundancy, and Cross Talk -- PCNA Structure and Interactions with Partner Proteins -- Peptide Pheromones and their Protein Receptors: Cellular Signaling in Gram-positive Bacteria -- Phagocytosis -- Plant Genome Sequencing Methods -- Plant Genomes: From Sequence to Function Across Evolutionary Time -- Plant Transposable Elements: Beyond Insertions and Interruptions -- Plasmid Cloning Vectors -- Plasmid Genomes, Introduction to -- Plasmid Incompatibility -- Plasmids as Secondary Chromosomes -- Polyglutamine Folding Diseases -- Polymerase Chain Reaction -- Practical Screening for DNA Damage -- Predictions from Sequence -- Primary Structure -- Prokaryotic Gene Regulation by Sigma Factors and RNA Polymerase -- Prokaryotic Gene Regulation by Small RNAs -- Protein Domain Structure Evolution -- Rad51 and Dmc1 Recombinases -- Reactive Oxygen Species -- Recombination: Mechanisms, Pathways, and Applications -- Recombineering -- Regulation of cytoplasmic mRNA -- Regulation of DSB Repair by Cell-cycle Signaling and the DNA Damage Response -- Regulation of Genetic Element Mobility -- Relevance of DNA Damage to Cancer -- Repeating Sequences in Proteins: Their Identification and Structural/Functional Implications -- Replication Origin of E. coli and the Mechanism of Initiation -- Replicative DNA Helicases and Primases -- Resolution of Inflammation -- Restriction Endonucleases -- RNA Interference -- RNA Quality Control -- RNA-induced chromatin remodeling -- Role of Chromatin Remodeling and DNA Modification in Transcriptional Regulation -- Roles of Post-translational Modifications in DNA Double Strand Break Repair -- Rolling-circle Replicating Plasmids -- Secondary Structure -- Selection with Antibiotics -- Selectivity of Chemicals for DNA Damage -- Sequence Selectivity of DNA Damage -- Signal Recognition in Lower Organisms: Light-Induced Control of Cell Movement in the Ciliates Blepharisma and Stentor -- SIKE: Discovery, Structure, and Function -- Single Strand Annealing -- Site-specific Mutagenesis -- Some Key Enzymes Used in Cloning -- Spectroscopy of Damaged DNA -- Synthesis of Modified Oligonucleotides -- Synthetic Plasmid Biology -- TANK-Binding Kinase 1 (TBK1): Structure, Function, and Regulation -- Target-primed Mobilization Mechanisms -- Target-site Selection -- Tertiary Structure Domains, Folds and Motifs -- The Complement System -- Theoretical Aspects of Secondary Structure -- Toll-Like Receptor 3: Structure and Function -- Toll-Like Receptors: Evolution and Structure -- Toll-Like Receptors: Pathogen Recognition and Signaling -- Topoisomerases and Cancer -- Transcription Factor Classes -- Transduction of Environmental Signals by Prokaryotic Two Component Regulatory Systems -- Transposable elements and plasmid genomes -- Transposons -- Types of DNA damage -- Types of Electrophiles -- Ultraviolet Light Damage -- uORFs: an unusual cis element that regulates translation -- Using Sequence Information to Assess Evolutionary Relationships -- Using Sequence Information to Identify Motifs -- V(D)J Recombination -- Why Do Proteins Have Quaternary Structure: Non-allosteric Proteins. |
| Record Nr. | UNINA-9910298413303321 |
| New York, NY : , : Springer New York : , : Imprint : Springer, , 2018 | ||
| Materiale a stampa | ||
| Lo trovi qui: Univ. Federico II | ||
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