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図書

図書
Roel Prins ... [et al]
出版情報: Hackensack, New Jersey : World Scientific, c2022  xviii, 392 p. ; 24 cm
シリーズ名: Advanced textbooks in chemistry
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Preface
About the Authors
Introduction / 1:
Catalysis and Catalysts / 1.1:
Heterogeneous and Homogeneous Catalysis / 1.2:
Production of Ammonia / 1.3:
Kinetics and Thermodynamics / 1.3.1:
Activity, Selectivity and Stability / 1.3.2:
H2 Production / 1.3.3:
Ammonia Synthesis / 1.3.4:
Relevance of Catalysis / 1.4:
References
Questions
Catalyst Preparation and Characterisation / 2:
Supported Catalysts / 2.1:
Crystal Structures / 2.2:
Crystal Lattices / 2.2.1:
X-ray Diffraction / 2.2.2:
Aluminas / 2.3:
Aluminium Hydroxides and Oxyhydroxides / 2.3.1:
Transition Aluminas / 2.3.2:
¿-Al2O3 / 2.3.3:
Surface of ¿-Al2O3 / 2.3.4:
Lewis acid sites / 2.3.5.1:
Brønsted acid sites / 2.3.5.2:
Surface reconstruction / 2.3.5.3:
Silica / 2.4:
Preparation of Supported Catalysts / 2.5:
Adsorption / 3:
Physisorption / 3.1:
Adsorption on Surfaces / 3.1.1:
Langmuir Adsorption Isotherm / 3.1.2:
Multilayer Adsorption, BET / 3.1.3:
Surface Diffusion / 3.2:
Chemisorption / 3.3:
Chemical Bonding / 3.3.1:
Dissociative Chemisorption / 3.3.2:
Kinetics / 4:
Langmuir-Hinshelwood Model / 4.1:
Monomolecular Reaction / 4.1.1:
Surface reaction is rate-determining / 4.1.1.1:
Adsorption of the reactant or product is rate-determining / 4.1.1.2:
Bimolecular Reaction / 4.1.2:
Influence of Diffusion / 4.2:
Bifunctional Catalysis / 4.3:
Metal Surfaces / 5:
Surface Structures / 5.1:
Surface Analysis / 5.2:
X-ray Photoelectron Spectroscopy / 5.2.1:
Auger Electron Spectroscopy / 5.2.2:
Surface Sensitivity / 5.2.3:
Surface Enrichment / 5.3:
Metal Binding / 5.4:
Metal Catalysis / 6:
Dissociation of H2 / 6.1:
Hydrogenation of Ethene / 6.2:
Synthesis of CO and H2 / 6.3:
Hydrogenation of CO / 6.4:
CO Hydrogenation to Hydrocarbons / 6.4.1:
CO dissociation / 6.4.1.1:
Methanation / 6.4.1.2:
Fischer-Tropsch reaction / 6.4.1.3:
Hydrogenation of CO and CO2 to Methanol / 6.4.2:
CO hydrogenation to methanol / 6.4.2.1:
CO2 hydrogenation to methanol / 6.4.2.2:
Hydrogenation of N2 to Ammonia / 6.5:
Fe Catalyst / 6.5.1:
Ru Catalyst / 6.5.2:
Volcano Curves / 6.6:
Catalysis by Solid Acids / 7:
Solid Acid Catalysts / 7.1:
Zeolites / 7.1.1:
Amorphous Silica-Alumina / 7.1.2:
Reactions of Hydrocarbons / 7.2:
Reactions of Alkenes and Alkanes / 7.2.1:
Isomerisation of Pentane, Hexane and Butene / 7.2.2:
Alcohols from Alkenes / 7.3:
Alkylation of Aromatics / 7.4:
Ethylation and Propylation of Benzene / 7.4.1:
Methylation of Toluene / 7.4.2:
Isomerisation, Disproportionation, Transalkylation / 7.4.3:
Gasoline Production / 7.5:
Fluid Catalytic Cracking and Hydrocracking / 7.5.1:
Methanol to Hydrocarbons / 7.5.2:
Reforming of Hydrocarbons by Bifunctional Catalysis / 7.5.3:
Cleaning of Fuels by Hydrotreating / 8:
Hydrotreating / 8.1:
Hydrotreating Catalysts / 8.2:
Metal Sulfides / 8.2.1:
Structure of sulfided Co-Mo/Al2O3 and Ni-Mo/Al2O3 / 8.2.1.1:
Active sites / 8.2.1.2:
Metal Phosphides / 8.2.2:
Reaction Mechanisms / 8.3:
Hydro desulfurisation / 8.3.1:
Hydrodenitrogenation / 8.3.2:
Hydrodeoxygenation / 8.3.3:
Hydrotreating of Mixtures / 8.3.4:
Hydrotreating Processes / 8.4:
Hydrodesulfurisation of Naphtha / 8.4.1:
Hydrotreating of Diesel / 8.4.2:
Residue Hydro conversion / 8.4.3:
Oxidation Catalysis / 9:
CO Oxidation / 9.1:
Mechanism / 9.1.1:
Three-way Catalysis / 9.1.2:
Production of Sulfuric and Nitric Acid / 9.2:
Sulfuric Acid / 9.2.1:
Nitric Acid / 9.2.2:
Selective Catalytic Reduction / 9.2.3:
Oxidation of Hydrocarbons / 9.3:
Oxidation by Oxygen / 9.3.1:
Oxidation by Hydroperoxide / 9.3.2:
Selective Partial Oxidation of Hydrocarbons / 9.3.3:
Oxidation of propene to acrylic acid and acrylonitrile / 9.3.3.1:
Oxidation of C4 and C6 molecules / 9.3.3.2:
Platform Chemicals / 9.4:
Electrocatalysis / 10:
Fundamental Aspects / 10.1:
Electrochemical Cells / 10.2.1:
Cell and Electrode Potentials / 10.2.2:
The Nernst Equation / 10.2.3:
Overpotential / 10.2.4:
Electrode Kinetics / 10.2.5:
Experimental Methods and Techniques / 10.3:
Three-Electrode Cell Configuration / 10.3.1:
Techniques for Electrocatalyst Evaluation / 10.3.2:
Linear Sweep Voltammetry and Cyclic Voltammetry / 10.3.3:
Electrochemical Impedance Spectroscopy / 10.3.4:
Rotating Disc Electrode / 10.3.5:
The Electro chemically Active Surface Area / 10.3.6:
Electrocatalysis for the Production of Sustainable Fuels and Chemicals / 10.4:
Development of Electrocatalysts / 10.4.1:
Hydrogen Evolution Reaction / 10.4.2:
Oxygen Evolution Reaction / 10.4.3:
CO2 Electroreduction / 10.4.4:
Other Electrochemical Processes / 10.4.5:
Answers
Index
Preface
About the Authors
Introduction / 1:
2.

図書

図書
Jesse M. Kinder and Philip Nelson
出版情報: Princeton : Princeton University Press, c2021  xiii, 223 p. ; 26 cm
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Let's Go
Getting Started with Python / 1:
Algorithms and algorithmic thinking / 1.1:
Algorithmic thinking / 1.1.1:
States / 1.1.2:
What does a = a + 1 mean? / 1.1.3:
Symbolic versus numerical / 1.1.4:
Launch Python / 1.2:
IPython console / 1.2.1:
Error messages / 1.2.2:
Sources of help / 1.2.3:
Good practice: Keep a log / 1.2.4:
Python modules / 1.3:
Import / 1.3.1:
From … import / 1.3.2:
NumPy and PyPlot / 1.3.3:
Python expressions / 1.4:
Numbers / 1.4.1:
Arithmetic operations and predefined functions / 1.4.2:
Good practice: Variable names / 1.4.3:
More about functions / 1.4.4:
Organizing Data / 2:
Objects and their methods / 2.1:
Lists, tuples, and arrays / 2.2:
Creating a list or tuple / 2.2.1:
NumPy arrays / 2.2.2:
Filling an array with values / 2.2.3:
Concatenation of arrays / 2.2.4:
Accessing array elements / 2.2.5:
Arrays and assignments / 2.2.6:
Slicing / 2.2.7:
Flattening an array / 2.2.8:
Reshaping an array / 2.2.9:
T2 Lists and arrays as indices / 2.2.10:
Strings / 2.3:
Raw strings / 2.3.1:
Formatting strings with the format () method / 2.3.2:
T2 Formatting strings with % / 2.3.3:
Structure and Control / 3:
Loops / 3.1:
For loops / 3.1.1:
While loops / 3.1.2:
Very long loops / 3.1.3:
Infinite loops / 3.1.4:
Array operations / 3.2:
Vectorizing math / 3.2.1:
Matrix math / 3.2.2:
Reducing an array / 3.2.3:
Scripts / 3.3:
The Editor / 3.3.1:
T2 Other editors / 3.3.2:
First steps to debugging / 3.3.3:
Good practice: Commenting / 3.3.4:
Good practice: Using named parameters / 3.3.5:
Good practice: Units / 3.3.6:
Contingent behavior: Branching / 3.4:
The if statement / 3.4.1:
Testing equality of floats / 3.4.2:
Nesting / 3.5:
Data In, Results Out / 4:
Importing data / 4.1:
Obtaining data / 4.1.1:
Bringing data into Python / 4.1.2:
Exporting data / 4.2:
Data files / 4.2.1:
Visualizing data / 4.3:
The plot command and its relatives / 4.3.1:
Log axes / 4.3.2:
Manipulate and embellish / 4.3.3:
Replacing curves / 4.3.4:
T2 More about figures and their axes / 4.3.5:
T2 Error bars / 4.3.6:
3D graphs / 4.3.7:
Multiple plots / 4.3.8:
Subplots / 4.3.9:
Saving figures / 4.3.10:
T2 Using figures in other applications / 4.3.11:
First Computer Lab / 5:
HIV example / 5.1:
Explore the model / 5.1.1:
Fit experimental data / 5.1.2:
Bacterial example / 5.2:
Random Number Generation and Numerical Methods / 5.2.1:
Writing your own functions / 6.1:
Defining functions in Python / 6.1.1:
Updating functions / 6.1.2:
Arguments, keywords, and defaults / 6.1.3:
Return values / 6.1.4:
Functional programming / 6.1.5:
Random numbers and simulation / 6.2:
Simulating coin flips / 6.2.1:
Generating trajectories / 6.2.2:
Histograms and bar graphs / 6.3:
Creating histograms / 6.3.1:
Finer control / 6.3.2:
Contour plots, surface plots, and heat maps / 6.4:
Generating a grid of points / 6.4.1:
Contour plots / 6.4.2:
Surface plots / 6.4.3:
Heat maps / 6.4.4:
Numerical solution of nonlinear equations / 6.5:
General real functions / 6.5.1:
Complex roots of polynomials / 6.5.2:
Solving systems of linear equations / 6.6:
Numerical integration / 6.7:
Integrating a predefined function / 6.7.1:
Integrating your own function / 6.7.2:
Oscillatory integrands / 6.7.3:
T2 Parameter dependence / 6.7.4:
Numerical solution of differential equations / 6.8:
Reformulating the problem / 6.8.1:
Solving an ODE / 6.8.2:
Other ODE solvers / 6.8.3:
Vector fields and streamlines / 6.9:
Vector fields / 6.9.1:
Streamlines / 6.9.2:
Second Computer Lab / 7:
Generating and plotting trajectories / 7.1:
Plotting the displacement distribution / 7.2:
Rare events / 7.3:
The Poisson distribution / 7.3.1:
Waiting times / 7.3.2:
Images and Animation / 8:
Image processing / 8.1:
Images as NumPy arrays / 8.1.1:
Saving and displaying images / 8.1.2:
Manipulating images / 8.1.3:
Displaying data as an image / 8.2:
Animation / 8.3:
Creating animations / 8.3.1:
Saving animations / 8.3.2:
HTML movies
T2 Using an encoder
Conclusion / 8.3.3:
Third Computer Lab / 9:
Convolution / 9.1:
Python tools for image processing / 9.1.1:
Averaging / 9.1.2:
Smoothing with a Gaussian / 9.1.3:
Denoising an image / 9.2:
Emphasizing features / 9.3:
T2 Image files and arrays / 9.4:
Advanced Techniques / 10:
Dictionaries and generators / 10.1:
Dictionaries / 10.1.1:
Special function arguments / 10.1.2:
List comprehensions and generators / 10.1.3:
Tools for data science / 10.2:
Series and data frames with pandas / 10.2.1:
Machine learning with scikit-learn / 10.2.2:
Next steps / 10.2.3:
Symbolic computing / 10.3:
Wolfram Alpha / 10.3.1:
The SymPy library / 10.3.2:
Other alternatives / 10.3.3:
First passage revisited / 10.3.4:
Writing your own classes / 10.4:
A random walk class / 10.4.1:
When to use classes / 10.4.2:
Get Going
Installing Python / A:
Install Python and Spyder / A.1:
Graphical installation / A.1.1:
Command line installation / A.1.2:
Setting up Spyder / A.2:
Working directory / A.2.1:
Interactive graphics / A.2.2:
Script template / A.2.3:
Restart / A.2.4:
Keeping up to date / A.3:
Installing FFmpeg / A.4:
Installing ImageMagick / A.5:
Command Line Tools / B:
The command line / B.1:
Navigating your file system / B.1.1:
Creating, renaming, moving, and removing files / B.1.2:
Creating and removing directories / B.1.3:
Python and Conda / B.1.4:
Text editors / B.2:
Version control / B.3:
How Git works / B.3.1:
Installing and using Git / B.3.2:
Tracking changes and synchronizing repositories / B.3.3:
Summary of useful workflows / B.3.4:
Troubleshooting / B.3.5:
Jupyter Notebooks / B.4:
Getting started / C.1:
Launch Jupyter Notebooks / C.1.1:
Open a notebook / C.1.2:
Multiple notebooks / C.1.3:
Quitting Jupyter / C.1.4:
T2 Setting the default directory / C.1.5:
Cells / C.2:
Code cells / C.2.1:
Graphics / C.2.2:
Markdown cells / C.2.3:
Edit mode and command mode / C.2.4:
Sharing / C.3:
More details / C.4:
Pros and cons / C.5:
Errors and Error Messages / D:
Python errors in general / D.1:
Some common errors / D.2:
Python 2 versus Python 3 / E:
Division / E.1:
Print command / E.2:
User input / E.3:
More assistance / E.4:
Under the Hood / F:
Assignment statements / F.1:
Memory management / F.2:
Functions / F.3:
Scope / F.4:
Name collisions / F.4.1:
Variables passed as arguments / F.4.2:
Summary / F.5:
Answers to "Your Turn" Questions / G:
Acknowledgments
Recommended Reading
Index
Let's Go
Getting Started with Python / 1:
Algorithms and algorithmic thinking / 1.1:
3.

図書

図書
E2S2-CREATE and AIChE Waste Management Conference ; American Institute of Chemical Engineers ; E2S2-CREATE
出版情報: New York : AIChE , Red Hook, NY : Printed from e-media with permission by Curran Associates, 2021, c2019  62 p. ; 28 cm
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4.

図書

図書
Rosette M. Roat-Malone
出版情報: Hoboken, N.J. : John Wiley & Sons, c2020  xxii, 328 p. ; 23 cm
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Preface
Acknowledgments
Biography
About the Companion Page
Inorganic Chemistry And Biochemistry Essentials / 1:
Introduction / 1.1:
Essential Chemical Elements / 1.2:
Inorganic Chemistry Basics / 1.3:
Electronic and Geometric Structures of Metals in Biological Systems / 1.4:
Thermodynamics and Kinetics / 1.5:
Bioorganometallic Chemistry / 1.6:
Inorganic Chemistry Conclusions / 1.7:
Introduction to Biochemistry / 1.8:
Proteins / 1.9:
Amino Acid Building Blocks / 1.9.1:
Protein Structure / 1.9.2:
Protein Function, Enzymes, and Enzyme Kinetics / 1.9.3:
DNA and RNA Building Blocks / 1.10:
DNA and RNA Molecular Structures / 1.10.1:
Transmission of Genetic Information / 1.10.2:
Genetic Mutations and Site-Directed Mutagenesis / 1.10.3:
Genes and Cloning / 1.10.4:
Genomics and the Human Genome / 1.10.5:
CRISPR / 1.10.6:
A Descriptive Example: Electron Transport Through DNA / 1.11:
Cyclic Voltammetry / 1.11.1:
Summary and Conclusions / 1.12:
Questions and Thought Problems / 1.13:
References
Computer Hardware, Software, Computational Chemistry Methods / 2:
Introduction to Computer-Based Methods / 2.1:
Computer Hardware / 2.2:
Computer Software for Chemistry / 2.3:
Chemical Drawing Programs / 2.3.1:
Visualization Programs / 2.3.2:
Computational Chemistry Software / 2.3.3:
Molecular Dynamics (MD) Software / 2.3.3.1:
Mathematical and Graphing Software / 2.3.3.2:
Molecular Mechanics (MM), Molecular Modeling, and Molecular Dynamics (MD) / 2.4:
Quantum Mechanics-Based Computational Methods / 2.5:
Ab-Initio Methods / 2.5.1:
Semiempirical Methods / 2.5.2:
Density Functional Theory and Examples / 2.5.3:
Starting with Schrödinger / 2.5.3.1:
Density Functional Theory (DFT) / 2.5.3.2:
Basis Sets / 2.5.3.3:
DFT Applications / 2.5.3.4:
Quantum Mechanics/Molecular Mechanics (QM/MM) Methods / 2.5.4:
Conclusions on Hardware, Software, and Computational Chemistry / 2.6:
Databases, Visualization Tools, Nomenclature, and other Online Resources / 2.7:
Important Metal Centers In Proteins / 2.8:
Iron Centers in Myoglobin and Hemoglobin / 3.1:
Structure and Function as Determined by X-ray Crystallography and Nuclear Magnetic Resonance / 3.1.1:
Cryo-Electron Microscopy and Hemoglobin Structure/Function / 3.1.3:
Cryo-Electron Microscopy Techniques / 3.1.3.1:
Structures Determined Using Cryo-Electron Microscopy / 3.1.3.3:
Model Compounds / 3.1.4:
Blood Substitutes / 3.1.5:
Iron Centers in Cytochromes / 3.2:
Cytochrome c Oxidase / 3.2.1:
Cytochrome c Oxidase (CcO) Structural Studies / 3.2.2:
Cytochrome c Oxidase (CcO) Catalytic Cycle and Energy Considerations / 3.2.3:
Proton Channels in Cytochrome c Oxidase / 3.2.4:
Cytochrome c Oxidase Model Compounds / 3.2.5:
Iron-Sulfur Clusters in Nitrogenase / 3.3:
Nitrogenase Structure and Catalytic Mechanism / 3.3.1:
Mechanism of Dinitrogen (N2) Reduction / 3.3.3:
Substrate Pathways into Nitrogenase / 3.3.4:
Nitrogenase Model Compounds / 3.3.5:
Functional Nitrogenase Models / 3.3.5.1:
Structural Nitrogenase Models / 3.3.5.2:
Copper and Zinc in Superoxide Dismutase / 3.4:
Superoxide Dismutase Structure and Mechanism of Catalytic Activity / 3.4.1:
A Copper Zinc Superoxide Dismutase Model Compound / 3.4.3:
Methane Monooxygenase / 3.5:
Soluble Methane Monooxygenase / 3.5.1:
Particulate Methane Monooxygenase / 3.5.3:
Hydrogenases, Carbonic Anhydrases, Nitrogen Cycle Enzymes / 3.6:
Hydrogenases / 4.1:
[NiFe]-hydrogenases / 4.2.1:
[NiFe]-hydrogenase Model Compounds / 4.2.2.1:
[FeFe]-hydrogenases / 4.2.3:
[FeFe]-Hydrogenase Model Compounds / 4.2.3.1:
[Fe]-hydrogenases / 4.2.4:
[Fe]-Hydrogenase Model Compounds / 4.2.4.1:
Carbonic Anhydrases / 4.3:
Carbonic Anhydrase Inhibitors / 4.3.1:
Nitrogen Cycle Enzymes / 4.4:
Nitric Oxide synthase / 4.4.1:
Nitric Oxide Synthase Structure / 4.4.2.1:
Nitric Oxide Synthase Inhibitors / 4.4.2.3:
Nitrite Reductase / 4.4.3:
Reduction of Nitrite Ion to Ammonium Ion / 4.4.3.1:
Reduction of Nitrite Ion to Nitric Oxide / 4.4.3.3:
Nanobioinorganic Chemistry / 4.5:
Introduction to Nanomaterials / 5.1:
Analytical Methods / 5.2:
Microscopy / 5.2.1:
Scanning Electron Microscopy (SEM) / 5.2.1.1:
Transmission Electron Microscopy (TEM) / 5.2.1.2:
Scanning Transmission Electron Microscopy (STEM) / 5.2.1.3:
Cryo-Electron Microscopy / 5.2.1.4:
Scanning Probe Microscopy (SPM) / 5.2.1.5:
Atomic Force Microscopy (AFM) / 5.2.1.6:
Super-Resolution Microscopy and DNA-PAINT / 5.2.1.7:
Förster Resonance Energy Transfer (FRET) / 5.2.2:
DNA Origami / 5.3:
Metallized DNA Nanomaterials / 5.4:
DNA-Coated Metal Electrodes / 5.4.1:
Plasmonics and DNA / 5.4.3:
Bioimaging with Nanomaterials, Nanomedicine, and Cytotoxicity / 5.5:
Imaging with Nanomaterials / 5.5.1:
Bioimaging using Quantum Dots (QD) / 5.5.3:
Nanoparticles in Therapeutic Nanomedicine / 5.5.4:
Clinical Nanomedicine / 5.5.4.1:
Some Drugs Formulated into Nanomaterials for Cancer Treatment: Cisplatinum, Platinum(IV) Prodrugs, and Doxorubicin / 5.5.4.2:
Theranostics / 5.6:
Nanoparticle Toxicity / 5.7:
Metals In Medicine, Disease States, Drug Development / 5.8:
Platinum Anticancer Agents / 6.1:
Cisplatin / 6.1.1:
Cisplatin Toxicity / 6.1.1.1:
Mechanism of Cisplatin Activity / 6.1.1.2:
Carboplatin (Paraplatin) / 6.1.2:
Oxaliplatin / 6.1.3:
Other cis-Platinum(II) Compounds / 6.1.4:
Nedaplatin / 6.1.4.1:
Lobaplatin / 6.1.4.2:
Heptaplatin / 6.1.4.3:
Antitumor Active Trans Platinum compounds / 6.1.5:
Platinum Drug Resistance / 6.1.6:
Combination Therapies: Platinum-Containing Drugs with Other Antitumor Compounds / 6.1.7:
Platinum(IV) Antitumor Drugs / 6.1.8:
Satraplatin / 6.1.8.1:
Ormaplatin / 6.1.8.2:
Iproplatin, JM9, CHIP / 6.1.8.3:
Platinum(TV) Prodrugs / 6.1.9:
Multitargeted Platinum(IV) Prodrugs / 6.1.9.1:
Platinum(IV) Prodrugs Delivered via Nanoparticles / 6.1.9.2:
Ruthenium Compounds as Anticancer Agents / 6.2:
Ruthenium(III) Anticancer Agents / 6.2.1:
Ruthenium(II) Anticancer Agents / 6.2.2:
Mechanism of Ruthenium(II) Anticancer Agent Activity / 6.2.3:
Ruthenium Compounds Tested for Antitumor Activity / 6.2.4:
Iridium and Osmium Antitumor Agents / 6.3:
Other Antitumor Agents / 6.4:
Gold Complexes / 6.4.1:
Titanium Complexes / 6.4.2:
Copper Complexes / 6.4.3:
Bismuth Derivatives as Antibacterials / 6.5:
Disease States, Drug Discovery, and Treatments / 6.6:
Superoxide Dismutases (SOD) in Disease States / 6.6.1:
Amyotrophic Lateral Sclerosis / 6.6.2:
Wilson's and Menkes Disease / 6.6.3:
Alzheimer's disease / 6.6.4:
Role of Amyloid ß Protein / 6.6.4.1:
Interactions of Aß Peptides with Metals / 6.6.4.2:
Alzheimer's Disease Treatments / 6.6.4.3:
Other Disease States Involving Metals / 6.7:
Copper and Zinc Ions and Cataract Formation / 6.7.1:
As2O3, used in the Treatment of Acute Promyelocytic Leukemia (APL) / 6.7.2:
Vanadium-based Type 2 Diabetes Drugs / 6.7.3:
Index / 6.8:
Preface
Acknowledgments
Biography
5.

図書

図書
Offshore Technology Conference
出版情報: Richardson, Tex. : Offshore Technology Conference , Red Hook, NY : Printed by Curran Associates, 2022  p. 714-1429 ; 28 cm
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6.

図書

図書
International Conference on Microbiome Engineering ; American Institute of Chemical Engineers
出版情報: New York : AIChE , Red Hook, NY : Printed from e-media with permission by Curran Associates, 2020. c2019  [3], 40, [2] p. ; 28 cm
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7.

図書

図書
National Conference on Artificial Intelligence ; Association for the Advancement of Artificial Intelligence
出版情報: Palo Alto, Calif. : Association for the Advancement of Artificial Intelligence , Red Hook, NY : Printed with permission by Curran Associates, 2021  p. 1343-1797 ; 27 cm
シリーズ名: 35th AAAI Conference on Artificial Intelligence (AAAI-21) : online 2-9 February 2021 ; v. 2
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8.

図書

図書
edited by Robert M Glaeser, Eva Nogales, Wah Chiu
出版情報: Bristol : IOP Publishing, c2021  1 v. ; 27 cm
シリーズ名: Biophysical Society-IOP series
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Editor biographies
Section authors
Introduction and overview / 1:
Visualizing biological molecules to understand life's principles / 1.1:
A brief historical perspective on scattering-based structural biology methods / 1.1.1:
Unique capabilities of cryo-EM: polymers and viruses / 1.1.2:
Unique capabilities of cryo-EM: integral membrane proteins / 1.1.3:
Unique capabilities of cryo-EM: large assemblies / 1.1.4:
Unique capabilities of cryo-EM: scarce samples / 1.1.5:
Unique capabilities of cryo-EM: compositionally heterogeneous samples / 1.1.6:
Unique capabilities of cryo-EM: conformationally complex samples / 1.1.7:
Current limits of cryo-EM and things yet to come / 1.1.8:
Recovery of 3D structures from images of weak-phase objects / 1.2:
The signal that we care about is attributed to elastic scattering of electrons / 1.2.1:
The electron accumulates information as it passes through a specimen / 1.2.2:
The image wave function, and thus the image intensity, suffers from imperfections in the microscope optics / 1.2.3:
Intermediate summary: the image intensity is linear in the projected Coulomb potential of the object / 1.2.4:
Structure-factor phases, as well as amplitudes, are retained in the computed Fourier transforms of image intensities / 1.2.5:
The projection theorem: the Fourier transform of an image corresponds to a 2D 'central' section within the 3D Fourier transform of the object / 1.2.6:
The 3D object can be reconstructed from multiple projections / 1.2.7:
Similarities and differences between sub-tomogram averaging and single-particle cryo-EM / 1.2.8:
References
Sample preparation / 2:
Overview / 2.1:
Initial screening of samples in negative stain / 2.2:
Introduction / 2.2.1:
Negative staining for TEM / 2.2.2:
Purpose of negative staining when starting a project / 2.2.3:
Techniques for the preparation of negatively stained samples / 2.2.4:
Use of data processing to provide feedback to optimize samples for cryo-EM / 2.2.5:
Standard method of making grids for cryo-EM / 2.3:
Grids and support films / 2.3.1:
Plasma cleaning or 'glow discharging' grids / 2.3.2:
Types of apparatus used for plunge freezing / 2.3.3:
Blotting and plunging the grid using plunge freezers / 2.3.4:
Common issues faced in making grids for cryo-EM imaging / 2.3.5:
Requirement to make very thin specimens for cryo-EM / 2.4:
Inelastic electron scattering causes the image quality to deteriorate with increasing sample thickness values / 2.4.1:
The projection approximation may fail if the sample is too thick / 2.4.2:
Areas of a grid where the sample is obviously too thick can, and should be, avoided during data collection / 2.4.3:
Areas where the sample is much too thin, perhaps even air-dried, can sometimes be avoided just on the basis of their subjective appearance / 2.4.4:
Current strategies for optimizing preparation of cryo-grids / 2.5:
Behavior of particles in the thin film environment / 2.5.1:
Approaches to alter particle behavior in the thin film / 2.5.2:
New technologies for sample preparation / 2.5.3:
Data collection / 3:
Radiation damage in cryo-EM / 3.1:
Interaction cross sections, elastic, and inelastic interactions / 3.2.1:
Cryoprotection and primary, secondary, and tertiary radiation damage / 3.2.3:
Radiation damage dependence on electron energy / 3.2.4:
Practical implications of radiation damage: image averaging in cryo-EM / 3.2.5:
Resolution dependence and exposure weighting / 3.2.6:
Radiation damage versus beam-induced motion and charging / 3.2.7:
Low-dose protocols for recording images / 3.3:
Automated low-dose imaging / 3.3.1:
Improving throughput / 3.3.2:
Electron exposure levels used during high-resolution data collection / 3.3.3:
Practical considerations: defocus. stigmation, coma-free illumination, and phase plates / 3.4:
Why do we need to defocus the microscope? / 3.4.1:
Effects of defocus on the image and its information content / 3.4.2:
Defocus variation is necessary to obtain uniform information coverage in reciprocal space / 3.4.3:
Optical correction of astigmatism and coma aberrations / 3.4.4:
Use of phase plates to improve image contrast and the expected benefits / 3.4.5:
Practical considerations: movie-mode data acquisition / 3.5:
Magnification and resolution / 3.5.1:
Dose rate / 3.5.2:
Strategies for motion correction / 3.5.3:
Total dose or exposure time / 3.5.4:
File size of movie datasets / 3.5.5:
Summary / 3.5.6:
Data processing / 4:
Automated extraction of particles / 4.1:
From micrographs to particles / 4.2.1:
Manual selection / 4.2.2:
Unbiased automated approaches / 4.2.3:
Particle extraction / 4.2.4:
Cleaning up the results through classification / 4.2.5:
CTF estimation and image correction (restoration) / 4.3:
CTF estimation / 4.3.1:
Image correction / 4.3.2:
Magnification distortion / 4.3.3:
Concluding remarks / 4.3.4:
Merging data from structurally homogeneous subsets / 4.4:
How many particle images are needed for a 3D reconstruction? / 4.4.1:
Obtaining a 3D reconstruction / 4.4.2:
Acknowledgments
3D classification of structurally heterogeneous particles / 4.5:
Global 3D classification / 4.5.1:
Masked 3D classification / 4.5.3:
3D classification of particles with pseudo-symmetry / 4.5.4:
Dealing with continuous motions / 4.5.5:
Conclusion / 4.5.6:
Preferred orientation: how to recognize and deal with adverse effects / 4.6:
Protein interaction with the air-water interface / 4.6.1:
Preferred orientation and its effects in cryo-EM / 4.6.2:
Quantifying preferred orientation and its effects on cryo-EM reconstructions / 4.6.3:
Overcoming the effects of preferred orientation / 4.6.4:
Areas of research / 4.6.5:
B factors and map sharpening / 4.7:
An ideal 3D reconstruction has a predictable radial amplitude spectrum / 4.7.1:
Actual 3D reconstructions feature dampened amplitudes at high frequencies / 4.7.2:
Several factors contribute to signal decay at high frequencies / 4.7.3:
Gaussian falloff, parametrized by a B factor, is a useful model of signal loss / 4.7.4:
Estimating B factors / 4.7.5:
Sharpening a map / 4.7.6:
A single inverse Gaussian filter using a global B factor does not always lead to the optimal map / 4.7.7:
Optical aberrations and Ewald sphere curvature / 4.8:
Further considerations on the aberration function ¿(s) / 4.8.1:
Common types of aberrations / 4.8.2:
Practical considerations for aberration correction / 4.8.3:
Thick objects and the Ewald sphere / 4.8.4:
Ewald sphere correction / 4.8.5:
Map validation / 5:
Measures of resolution: FSC and local resolution / 5.1:
The 'gold-standard' FSC / 5.2.1:
Resolution thresholds / 5.2.2:
FSC artifacts due to masking, filtration, and CTF / 5.2.3:
Local resolution / 5.2.4:
Resolution anisotropy / 5.2.5:
Recognizing the effect of bias and over-fitting / 5.3:
Introduction and nature of the problem arising from iterative refinement / 5.3.1:
Assessing the consistency of maps with projection data / 5.3.2:
Detecting over-fitting at high resolution in maps and effect on the FSC / 5.3.3:
Local over-fitting / 5.3.4:
Estimates of alignment accuracy / 5.3.5:
Correlation and the signal-to-noise ratio (SNR) / 5.4.1:
Analysis of alignment accuracy with synthetic data / 5.4.2:
The relationship between alignment accuracy and resolution / 5.4.3:
Estimating alignment accuracy from tilt pairs / 5.4.4:
Estimating alignment accuracy from the reconstructed map / 5.4.5:
Estimating alignment accuracy from projection-matching results / 5.4.6:
Discussion / 5.5:
Acknowledgements
Model building and validation / 6:
Using known components or homologs: model building / 6.1:
Identifying known/modeled structures of individual subunits / 6.2.1:
Rigid-body fitting / 6.2.2:
Flexible fitting / 6.2.3:
Building atomistic models in cryo-EM density maps / 6.3:
Building models into cryo-EM density maps / 6.3.1:
Model refinement / 6.3.3:
Model validation / 6.3.4:
Model uncertainty / 6.3.5:
Model deposition / 6.3.6:
Revisiting the cryo-EM model challenge / 6.3.7:
Toward the future / 6.3.8:
Conclusions / 6.3.9:
Quality evaluation of cryo-EM map-derived models / 6.4:
Map-model metrics / 6.4.1:
Model-only metrics / 6.4.3:
Summary and conclusions / 6.4.4:
Acknowledgment
How algorithms from crystallography are helping electron cryo-microscopy / 6.5:
Map improvement / 6.5.1:
Map interpretation and model building / 6.5.3:
Model optimization / 6.5.4:
Validation / 6.5.5:
Validation-guided corrections / 6.5.6:
Archiving structures and data / 6.5.7:
Single-particle cryo-EM structure deposition / 6.6.1:
Preparing files for deposition / 6.6.3:
Data validation / 6.6.4:
Sample sequence and ligands / 6.6.5:
Deposition using OneDep / 6.6.6:
Post-deposition: what happens next? / 6.6.7:
Accessing cryo-EM structure data / 6.6.8:
Editor biographies
Section authors
Introduction and overview / 1:
9.

図書

図書
SPE Technical Conference and Exhibition ; Society of Petroleum Engineers of AIME
出版情報: Richardson, Tex. : Society of Petroleum Engineers , Red Hook, NY : Printed from e-media with permission by Curran Associates, 2020, c2019  p. 737-1473 ; 28 cm
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10.

図書

図書
Svetlana Katok...[et al.]
出版情報: Hackensack, NJ : World Scientific Publishing Co. Pte. Ltd., c2024  lxxv, 1309-2540 p. ; 26 cm
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目次情報:
Cohomology and Geometric Rigidity
Measure Rigidity
Cohomology and Geometric Rigidity
Measure Rigidity
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