| Preface | p. xi |
| Contributors | p. xv |
| RAIRS under ultrahigh vacuum conditions on metal surfaces | p. 1 |
| Short history of RAIRS | p. 1 |
| How does it work - the physical basis of RAIRS | p. 2 |
| Description of apparatus and coupling with a UHV chamber | p. 8 |
| Selected examples. Why is RAIRS so successful for thin films on metal surfaces? | p. 8 |
| CO on pure metal surfaces: the beginning | p. 8 |
| Lysine and tartaric acid on Cu(1 1 0) single crystal surface; glutamic acid on Ag(1 10) | p. 11 |
| Bio-molecules (peptides) adsorbed on metal surfaces, studied by RAIRS | p. 19 |
| Conclusions | p. 24 |
| References | p. 25 |
| PM-1RRAS at liquid interfaces | p. 27 |
| Introduction | p. 27 |
| Principle, Theory And Experimental Setup | p. 28 |
| PM-IRRAS signal | p. 28 |
| Signal modelling: optimum angle of incidence and surface selection rule | p. 29 |
| Optimum angle of incidence | p. 29 |
| Surface selection rule | p. 31 |
| Experimental setup | p. 33 |
| Applications | p. 35 |
| Lipids | p. 35 |
| Bi and multilayers at the air-water interface | p. 37 |
| Peptides/ Interaction peptide-membrane | p. 38 |
| Gramicidin | p. 43 |
| Proteins/Interaction Protein-Membrane | p. 45 |
| Membraneous proteins | p. 45 |
| Other systems | p. 48 |
| DNA/cationic lipids interactions | p. 49 |
| Conclusions | p. 53 |
| References | p. 54 |
| Infrared spectroscopy for characterization of biomolecular interfaces | p. 57 |
| General Considerations for Semiconductor Surfaces | p. 59 |
| Absorption versus dispersion | p. 66 |
| Biological molecules at surfaces: nonspecific binding of fibrinogen on H-terminated silicon surfaces | p. 68 |
| Protein binding on a diamond thin film | p. 70 |
| Influence of substrate material on FTIR spectra | p. 73 |
| Conformational analysis of proteins on surfaces by FTIR | p. 78 |
| Conclusions and Outlook | p. 80 |
| Acknowledgments | p. 80 |
| References | p. 80 |
| Infrared analysis of biomolecule attachment of functionalized silicon surfaces | p. 83 |
| Introduction | p. 83 |
| Silicon surface functionalization | p. 88 |
| Functionalization of silicon oxide surfaces | p. 88 |
| Activation methods for optimal results | p. 90 |
| APS layer formation is highly dependent on atmospheric conditions | p. 92 |
| APS layer formation is highly uncontrolled and unstable in aqueous media | p. 93 |
| Functionalization of oxide-free silicon surfaces | p. 98 |
| Biotinylation | p. 100 |
| Behavior of Biotinylated Surfaces in Different Environments | p. 102 |
| Protein attachment | p. 106 |
| Behavior of the biotinylated surface upon protein adsorption | p. 107 |
| Biotinylation and protein attachment to oxide-free silicon surfaces | p. 107 |
| Conclusions | p. 110 |
| Acknowledgements | p. 112 |
| References | p. 112 |
| Attenuated total reflection infrared (ATR-IR) spectroscopy, modulation excitation spectroscopy (MES), and vibrational circular dichroism (VCD) | p. 115 |
| General Introduction | p. 115 |
| ATR-IR spectroscopy | p. 116 |
| Conclusions | p. 127 |
| MES | p. 128 |
| Conclusions | p. 137 |
| Vibrational Circular Dichroism (VCD) | p. 138 |
| Conclusions | p. 142 |
| Acknowledgment | p. 142 |
| References | p. 142 |
| Synchrotron infrared interface science | p. 145 |
| Introduction | p. 145 |
| Synchrotron infrared Emission | p. 147 |
| Infrared emission in storage rings | p. 148 |
| Synchrotron Infrared Studies in Surface Science | p. 154 |
| Identification of low frequency modes of adsorbed species | p. 155 |
| Vibrational dynamics | p. 156 |
| Synchrotron Infrared Applications in Biology | p. 157 |
| Single cells and tissues studies | p. 157 |
| Spatially resolved biomolecular interface study | p. 159 |
| Perspectives In Synchrotron Infrared for Biointerfaces | p. 162 |
| References | p. 164 |
| IR Spectroscopy for biorecognition and molecular sensing | p. 167 |
| Introduction | p. 168 |
| Surface IR Spectroscopy for The Label-free Detection biorecognition Events | p. 168 |
| The ATR technique | p. 168 |
| The SEIRAs technique | p. 176 |
| The IRRAS and PM-IRRAS techniques | p. 179 |
| Conclusion | p. 187 |
| Transition Metal Carbonyl (TMC) Probes | p. 188 |
| IR spectroscopy of metal carbonyls | p. 188 |
| Detection of biorecognition events by IR spectroscopy with TMC labels | p. 189 |
| Molecular sensing by IR spectroscopy | p. 204 |
| Non TMC probes for molecular sensing and biomolecular interaction studies | p. 208 |
| Conclusion | p. 212 |
| References | p. 213 |
| Advanced infrared glasses for biochemical sensing | p. 217 |
| Introduction | p. 217 |
| Overview | p. 217 |
| Development and historical background of FEWS | p. 219 |
| Instrument description | p. 220 |
| FEWS principle | p. 220 |
| Fiber sensor design | p. 221 |
| IR materials for FEWS | p. 224 |
| Application of FEWS to biosensing | p. 229 |
| Hydrophobic fiber surface for sensing in aqueous environments | p. 229 |
| Monitoring of live cells | p. 231 |
| Monitoring the dynamic of biofilms | p. 233 |
| Perspectives and Conclusions | p. 235 |
| Statistical spectral analysis | p. 235 |
| Biosensing through electrophoretic captureof charged molecules | p. 238 |
| Conclusion | p. 240 |
| Acknowledgments | p. 240 |
| References | p. 240 |
| AFM-IR: photothermal infrared nanospectroscopy | p. 245 |
| Introduction | p. 245 |
| Concept and Technique Description | p. 246 |
| AFM-IR setup description | p. 247 |
| Infrared absorption and spectroscopy | p. 248 |
| Photothermal effect | p. 249 |
| Thermoelasticity | p. 251 |
| AFM-IR formalisation | p. 252 |
| Applications In Microbiology: Bacteria Studies | p. 258 |
| Experimental demonstration on E. coli | p. 259 |
| T5 bacteriophage detection inside E. coli | p. 263 |
| PHB location into Rhodobacter capsulatus | p. 265 |
| Mapping Eukaryotes Using AFM-IR | p. 270 |
| Localization of the endogenous structure by AFMIR | p. 270 |
| Example of the localization of exogenous compounds | p. 271 |
| Conclusion | p. 276 |
| Acknowledgments | p. 276 |
| References | p. 276 |
| Sum frequency generation spectroscopy of biointerfaces | p. 279 |
| Introduction | p. 279 |
| Theoretical background, relevant properties and experimental setups for SFC spectroscopy | p. 283 |
| SFC basics | p. 283 |
| Experimental SFG setups | p. 290 |
| Examples of applications to biological interfaces | p. 295 |
| Lipid mono-and bilayers | p. 296 |
| Peptides and proteins | p. 300 |
| Biosensing | p. 306 |
| Prospects311 | |
| Dynamics and kinetics: from fast to ultrafast time resolution | p. 311 |
| Playing with colors and excited states: 2D-IR SFG, DR-SFC | p. 313 |
| SFG microscopy: towards high-resolution imaging of biointerfaces | p. 316 |
| Conclusions | p. 318 |
| References | p. 318 |
| Index | p. 323 |
| Table of Contents provided by Ingram. All Rights Reserved. |
