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1.

図書

図書
edited by Dietmar Hutmacher, Wojciech Chrzanowski
出版情報: Cambridge : Royal Society of Chemistry, c2015  xvi, 453 p. ; 24 cm
シリーズ名: RSC smart materials ; no. 10
2.

図書

図書
edited by Wolfgang Knoll
出版情報: Singapore : Pan Stanford, c2013  xxxi, 1125 p., 24 p. of plates ; 24 cm
目次情報: 続きを見る
Self-Assembled Monolayers (SAMs)
Multi-Valent Chelator SAMs
Gemini SAMs
PEG SAMs
Electrochemically Designed SAMs
Polymer Brushes
Ultra-Sensitive Biosensing with Polymer Brushes
Noncovalent Anchoring of Proteins to Surfaces
S-Layer Proteins
Heparan Sulfate Surfaces to Probe the Functions of the Master Regulator of the Extracellular Space
Hemocompatible Surfaces
Peptide Nanotube Coatings for Bioapplications
Proteoglycanylated Surfaces
Surface-Attached Polymeric Hydrogel Films
Evanescent Wave Biosensors with Hydrogels Binding Matrix
IPNs
Biofunctional Grafted Dendrons
Glucase Biosensors: Transduction Method, Redox Materials, and Bio-Interface
Modification of Glass Surfaces by Phosphorus Dendrimer Layers for Biosensors
Tethering Lipid Bilayers to Solid Supports
In vitro Synthesis of Membrane Proteins
Integrin-Functionalized Artificial Membranes as Test Platforms for Monitoring Small Integrin Ligand Binding by Surface Plasmon-Enhanced Fluorescence Spectroscopy
Wetting of Surfaces by Lipid Bilayers
Patterned Lipid Bilayers on Solid Substrate as a Model System of the Biological Membrane
Electrically Addressable, Biologically Relevant Surface Supported Bilayers
Nanopatterning of Biomolecules by Dip Pen Lithography
Surfaces for Stem Cell Propagation
Mechanical Cues for Cell Culture
Constructing Defined Networks of Neurons
Mineralization on a Biomimetic Surface
MO-CVD on patterned SAMs
Application of Biofunctional Surfaces in Medical Diagnostics
Nanopatterning for Bioapplications
Self-Assembled Monolayers (SAMs)
Multi-Valent Chelator SAMs
Gemini SAMs
3.

図書

図書
Otto G. Berg, Mahendra Kumar Jain
出版情報: Chichester : John Wiley & Sons, 2002  xxvi, 301 p. ; 25 cm
目次情報: 続きを見る
Preface
Theory Boxes
List of Symbols
Why Interfacial Enzymes? / 1:
Structural Diversity of Nonpolar and Amphiphilic Solutes / 1.1:
To Be or Not to Be in Water / 1.2:
The Hydrophobic Effect / 1.3:
Knotty Issues of Interfacial Enzymology / 1.4:
Pathophysiology of Lipolytic Enzymes / 1.5:
Secreted PLA2 (sPLA2) Prototype for Interfacial Enzymology / 1.6:
Summary and Outlook: Towards the Paradigm for Interfacial Enzymology / 1.7:
Further Reading
Interface Phenomena: Accessibility and Exchange / 2:
Aggregates and Dispersions / 2.1:
Organized Micellar Aggregates in Aqueous Dispersions / 2.2:
Amphiphile Organization and the Monomer-Micelle Equilibrium and Exchange / 2.3:
The Concentration Issues in the Monomer-Aggregate Equilibria / 2.4:
Exchange of Amphiphiles between Organized Interfaces / 2.5:
Dispersed Phases / 2.6:
Choice of Interface for Study of an Interfacial Enzyme / 2.7:
Summary: Interface Determines the Accessibility and Replenishment Rate / 2.8:
To Be or Not To Be: Dilemma for the Substrate in Solution / 3:
Constrained Reaction Path for the Turnover in the Aqueous Phase / 3.1:
Analysis of the Steady State Turnover Cycle in the Aqueous Phase / 3.2:
Ascertaining the Reaction Path in the Aqueous Phase / 3.3:
PAF-Acetylhydrolase Hydrolyzes the Monodisperse Substrate / 3.4:
Equilibrium Partitioning and Binding to Aggregates / 3.5:
Summary: The Equilibrium Dilemma / 3.6:
Interfacial Processivity: Ensemble Behavior in the Scooting Mode / 4:
Conceptualizing Interfacial Processivity / 4.1:
The Fourfold Meaning of the Substrate Concentration / 4.2:
Constraints for Defining the Variables for the Reaction Progress in the Scooting Mode / 4.3:
Integrity of Vesicles during the Scooting Mode Reaction Progress / 4.4:
Tests for the Scooting Mode Reaction Progress by PLA2 / 4.5:
Ensemble Behavior of the Binding of the Enzyme to Vesicles / 4.6:
Summary: Ensemble Behavior in a Microscopically Heterogeneous Environment / 4.7:
Analysis of the Processive Reaction Progress / 5:
Michaelis-Menten Equation for the Turnover in the Interface / 5.1:
Catalytic Parameters from the Integrated Processive Reaction Progress / 5.2:
Additional Constraints for the Analysis of the Interfacial Turnover Events for PLA2 / 5.3:
Uses of the Primary Catalytic Parameters / 5.4:
Catalytic Mechanism of PLA2 / 5.5:
The Quality-of-Interface Effects / 5.6:
Apparent Interfacial Activation / 5.7:
Hopping and the Fast Enzyme Exchange Limit / 5.8:
Summary: Variations in the Processivity / 5.9:
Detailed Balance Conditions for Interfacial Equilibria / 6:
Binding of Ions to the Interface / 6.1:
Equilibria for the Binding of the Enzyme to the Interface / 6.2:
Effective Equilibrium Constants / 6.3:
The Cofactor Binding Obligatory for the Substrate Binding / 6.4:
Detailed Balance Conditions and Local Concentrations for Effective Ligand Binding / 6.5:
Resolution of the Interfacial Constants for PLA2 / 6.6:
Detailed Balance Conditions for PLA2 / 6.7:
Summary: Primary Equilibrium Parameters for the Kinetic Path / 6.8:
Rapid Substrate Replenishment in the Quasi-Scooting Mode / 7:
Interfacial Catalytic Cycle Turnover in the Quasi-Scooting Mode / 7.1:
Sparingly Soluble Substrates / 7.2:
Reaction Rate with the Partitioned Substrate / 7.3:
Interfacial Turnover by Triglyceride Lipase / 7.4:
Lid on tl-Lipase Active Site / 7.5:
Interfacial Allostery for the Quality-of-Interface Effects / 7.6:
Motifs for Close Contact of Proteins with the Interface / 7.7:
Summary: Multiple States of the Enzyme at the Interface / 7.8:
Interfacial Allostery / 8:
Interfacial Catalytic Turnover in the Quasi-Scooting Mode / 8.1:
The Apparent Rate Parameters for the Pig Pancreatic PLA2 / 8.2:
K*[subscript S] Allosteric Effects of the Interface / 8.3:
Analysis of the Interfacial Anionic Charge Preference: k*[subscript catS] Activation / 8.4:
The Structural Basis for the Anionic Interface Preference / 8.5:
Modeling the i-face of PLA2 / 8.6:
Site-Directed Mutagenesis to Discern Interactions Along the i-face / 8.7:
Summary: Residues Involved in Charge Compensation / 8.8:
Inhibition: Specific or Nonspecific / 9:
Specific Inhibitors / 9.1:
Kinetic Effects of Nonspecific Inhibitors / 9.2:
Kinetic Effects of the Interface-Based Competitive Inhibitors / 9.3:
Influence of Cofactor on the Scooting Kinetics / 9.4:
Effects of the Interface-Based Inhibitor on the Integrated Rate Equation in the Scooting Mode / 9.5:
Partitioning of the Inhibitor and Substrate between the Interface and the Aqueous Phase / 9.6:
Summary: Multiple Pathways for Reduction of the Observed Rate / 9.7:
The Delay to the Steady State in the Reaction Progress / 10:
Effects of the Accumulated Products in Zwitterionic Bilayers / 10.1:
Model for the Delay Due to the Product Accumulation during the Reaction Progress on Phosphatidylcholine Vesicles / 10.2:
Effect of the Accumulated Products on the Delay in the Monolayer Reaction Progress / 10.3:
Summary: Activation by the Anionic Charge Induced by the Product Accumulation / 10.4:
Nonidealities of the Dispersed Phases / 11:
The Exchange Limit / 11.1:
Exchange-Limited Kinetics of PLA2 in Detergent-Dispersed Mixed Micelles of Long Chain Phospholipids / 11.2:
Effect of Bile Salts on the Pancreatic PLA2 Catalyzed Hydrolysis of Phosphatidylcholines / 11.3:
Kinetic Concerns for Interfaces of the Dispersed Phase / 11.4:
The Nonideality Factor / 11.5:
Summary: Nonidealities for Replenishment and Binding / 11.6:
Effects of Reduction of Dimensionality / 12:
Dissection of the Entropy Loss on Interface Binding / 12.1:
Synergistic Effects of the Interface on Enzyme-Substrate Binding, Local Concentration and Scaffolding / 12.2:
Diffusion Times in 1D, 2D and 3D / 12.3:
Rate Enhancement by Facilitated Diffusion in 2D / 12.4:
Summary: Dimensionality Effects on the Equilibrium and Diffusion / 12.5:
References
Index
Preface
Theory Boxes
List of Symbols
4.

図書

図書
edited by C.-M. Pradier, Y.J. Chabal
出版情報: Oxford : Elsevier, 2011  xvi, 327 p.: ill. ; 24 cm
目次情報: 続きを見る
Preface
Contributors
RAIRS under ultrahigh vacuum conditions on metal surfaces / V. Humblot ; C M. Pradier1:
Short history of RAIRS
How does it work - the physical basis of RAIRS
Description of apparatus and coupling with a UHV chamber
Selected examples. Why is RAIRS so successful for thin films on metal surfaces?
CO on pure metal surfaces: the beginning
Lysine and tartaric acid on Cu(1 1 0) single crystal surface; glutamic acid on Ag(1 10)
Bio-molecules (peptides) adsorbed on metal surfaces, studied by RAIRS
Conclusions
References
PM-1RRAS at liquid interfaces / D. Blaudez ; S. Castano ; B. Desbat2:
Introduction
Principle, Theory And Experimental Setup
PM-IRRAS signal
Signal modelling: optimum angle of incidence and surface selection rule
Optimum angle of incidence
Surface selection rule
Experimental setup
Applications
Lipids
Bi and multilayers at the air-water interface
Peptides/ Interaction peptide-membrane
Gramicidin
Proteins/Interaction Protein-Membrane
Membraneous proteins
Other systems
DNA/cationic lipids interactions
Infrared spectroscopy for characterization of biomolecular interfaces / R. j. Hamers ; X. Wang ; R. Franking ; R. Ruther ; C. Stavis3:
General Considerations for Semiconductor Surfaces
Absorption versus dispersion
Biological molecules at surfaces: nonspecific binding of fibrinogen on H-terminated silicon surfaces
Protein binding on a diamond thin film
Influence of substrate material on FTIR spectra
Conformational analysis of proteins on surfaces by FTIR
Conclusions and Outlook
Acknowledgments
Infrared analysis of biomolecule attachment of functionalized silicon surfaces / N. A. Lapin ; O. Seitz ; Y. J. Chabal4:
Silicon surface functionalization
Functionalization of silicon oxide surfaces
Activation methods for optimal results
APS layer formation is highly dependent on atmospheric conditions
APS layer formation is highly uncontrolled and unstable in aqueous media
Functionalization of oxide-free silicon surfaces
Biotinylation
Behavior of Biotinylated Surfaces in Different Environments
Protein attachment
Behavior of the biotinylated surface upon protein adsorption
Biotinylation and protein attachment to oxide-free silicon surfaces
Acknowledgements
Attenuated total reflection infrared (ATR-IR) spectroscopy, modulation excitation spectroscopy (MES), and vibrational circular dichroism (VCD) / T. Bürgi5:
General Introduction
ATR-IR spectroscopy
MES
Vibrational Circular Dichroism (VCD)
Acknowledgment
Synchrotron infrared interface science / P. Dumas6:
Synchrotron infrared Emission
Infrared emission in storage rings
Synchrotron Infrared Studies in Surface Science
Identification of low frequency modes of adsorbed species
Vibrational dynamics
Synchrotron Infrared Applications in Biology
Single cells and tissues studies
Spatially resolved biomolecular interface study
Perspectives In Synchrotron Infrared for Biointerfaces
IR Spectroscopy for biorecognition and molecular sensing / CM. Pradier ; M. Salmain ; S. Boujday7:
Surface IR Spectroscopy for The Label-free Detection biorecognition Events / Part I:
The ATR technique
The SEIRAs technique
The IRRAS and PM-IRRAS techniques
Conclusion
Transition Metal Carbonyl (TMC) Probes / Part II:
IR spectroscopy of metal carbonyls
Detection of biorecognition events by IR spectroscopy with TMC labels
Molecular sensing by IR spectroscopy
Non TMC probes for molecular sensing and biomolecular interaction studies
Advanced infrared glasses for biochemical sensing / P. Lucas ; B. Bureau8:
Overview
Development and historical background of FEWS
Instrument description
FEWS principle
Fiber sensor design
IR materials for FEWS
Application of FEWS to biosensing
Hydrophobic fiber surface for sensing in aqueous environments
Monitoring of live cells
Monitoring the dynamic of biofilms
Perspectives and Conclusions
Statistical spectral analysis
Biosensing through electrophoretic captureof charged molecules
AFM-IR: photothermal infrared nanospectroscopy / A. Dazzi ; C. Policar9:
Concept and Technique Description
AFM-IR setup description
Infrared absorption and spectroscopy
Photothermal effect
Thermoelasticity
AFM-IR formalisation
Applications In Microbiology: Bacteria Studies
Experimental demonstration on E. coli
T5 bacteriophage detection inside E. coli
PHB location into Rhodobacter capsulatus
Mapping Eukaryotes Using AFM-IR
Localization of the endogenous structure by AFMIR
Example of the localization of exogenous compounds
Sum frequency generation spectroscopy of biointerfaces / C. Humbert ; B. Busson10:
Theoretical background, relevant properties and experimental setups for SFC spectroscopy
SFC basics
Experimental SFG setups
Examples of applications to biological interfaces
Lipid mono-and bilayers
Peptides and proteins
Biosensing
Prospects311
Dynamics and kinetics: from fast to ultrafast time resolution
Playing with colors and excited states: 2D-IR SFG, DR-SFC
SFG microscopy: towards high-resolution imaging of biointerfaces
Index
Preface
Contributors
RAIRS under ultrahigh vacuum conditions on metal surfaces / V. Humblot ; C M. Pradier1:
5.

電子ブック

EB
Thomas Horbett, editor, John L. Brash, editor, Willem Norde, editor ; sponsored by the ACS Division of Colloid and Surface Chemistry
出版情報: [Washington, DC] : American Chemical Society, c2022  1 online resource (869 p.)
シリーズ名: ACS symposium series ; 1120
6.

図書

図書
edited by Michael L. Hair
出版情報: New York : M. Dekker, 1971-72  2 v ; 24 cm
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