Note: Intro -- Vibrational Spectroscopy in Life Science -- Contents -- Preface -- 1 Introduction -- 1.1 Aims of Vibrational Spectroscopy in Life Sciences -- 1.2 Vibrational Spectroscopy - An Atomic-scale Analytical Tool -- 1.3 Biological Systems -- 1.4 Scope of the Book -- 1.5 Further Reading -- References -- 2 Theory of Infrared Absorption and Raman Spectroscopy -- 2.1 Molecular Vibrations -- 2.1.1 Normal Modes -- 2.1.2 Internal Coordinates -- 2.1.3 The FG-Matrix -- 2.1.4 Quantum Chemical Calculations of the FG-Matrix -- 2.2 Intensities of Vibrational Bands -- 2.2.1 Infrared Absorption -- 2.2.2 Raman Scattering -- 2.2.3 Resonance Raman Effect -- 2.3 Surface Enhanced Vibrational Spectroscopy -- 2.3.1 Surface Enhanced Raman Effect -- 2.3.2 Surface Enhanced Infrared Absorption -- References -- 3 Instrumentation -- 3.1 Infrared Spectroscopy -- 3.1.1 Fourier Transform Spectroscopy -- 3.1.1.1 Interferometer -- 3.1.1.2 Infrared Detectors -- 3.1.2 Advantages of Fourier Transform Infrared Spectroscopy -- 3.1.3 Optical Devices: Mirrors or Lenses? -- 3.1.4 Instrumentation for Time-resolved Infrared Studies -- 3.1.4.1 Time-resolved Rapid-scan Fourier Transform Infrared Spectroscopy -- 3.1.4.2 Time-resolved Studies Using Tunable Monochromatic Infrared Sources -- 3.1.4.3 Time-resolved Fourier Transform Infrared Spectroscopy Using the Step-scan Method -- 3.1.5 Time-resolved Pump-probe Studies with Sub-nanosecond Time-resolution -- 3.2 Raman Spectroscopy -- 3.2.1 Laser -- 3.2.1.1 Laser Beam Properties -- 3.2.1.2 Optical Set-up -- 3.2.2 Spectrometer and Detection Systems -- 3.2.2.1 Monochromators -- 3.2.2.2 Spectrographs -- 3.2.2.3 Confocal Spectrometers -- 3.2.2.4 Fourier Transform Raman Interferometers -- References -- 4 Experimental Techniques -- 4.1 Inherent Problems of Infrared and Raman Spectroscopy in Life Sciences. , 4.1.1 The ''Water'' Problem in Infrared Spectroscopy -- 4.1.2 Unwanted Photophysical and Photochemical Processes in Raman Spectroscopy -- 4.1.2.1 Fluorescence and Raman Scattering -- 4.1.2.2 Photoinduced Processes -- 4.2 Sample Arrangements -- 4.2.1 IR Spectroscopy -- 4.2.1.1 Sandwich Cuvettes for Solution Studies -- 4.2.1.2 The Attenuated Total Reflection (ATR) Method -- 4.2.1.3 Electrochemical Cell for Infrared Spectroscopy -- 4.2.2 Raman and Resonance Raman Spectroscopy -- 4.2.2.1 Measurements in Solutions -- 4.2.2.2 Solid State and Low-temperature Measurements -- 4.3 Surface Enhanced Vibrational Spectroscopy -- 4.3.1 Colloidal Suspensions -- 4.3.2 Massive Electrodes in Electrochemical Cells -- 4.3.3 Metal Films Deposited on ATR Elements -- 4.3.4 Metal/Electrolyte Interfaces -- 4.3.5 Adsorption-induced Structural Changes of Biopolymers -- 4.3.6 Biocompatible Surface Coatings -- 4.3.7 Tip-enhanced Raman Scattering -- 4.4 Time-resolved Vibrational Spectroscopic Techniques -- 4.4.1 Pump-Probe Resonance Raman Experiments -- 4.4.1.1 Continuous-wave Excitation -- 4.4.1.2 Pulsed-laser Excitation -- 4.4.1.3 Photoinduced Processes with Caged Compounds -- 4.4.2 Rapid Mixing Techniques -- 4.4.2.1 Rapid Flow -- 4.4.2.2 Rapid Freeze-Quench -- 4.4.3 Relaxation Methods -- 4.4.4 Spatially Resolved Vibrational Spectroscopy -- 4.5 Analysis of Spectra -- References -- 5 Structural Studies -- 5.1 Basic Considerations -- 5.2 Practical Approaches -- 5.3 Studies on the Origin of the Sensitivity of Amide I Bands to Secondary Structure -- 5.4 Direct Measurement of the Interaction of the Amide I Oscillators -- 5.5 UV-resonance Raman Studies Using the Amide III Mode -- 5.6 Protein Folding and Unfolding Studies Using Vibrational Spectroscopy -- References -- 6 Retinal Proteins and Photoinduced Processes -- 6.1 Rhodopsin -- 6.1.1 Resonance Raman Studies of Rhodopsin. , 6.1.2 Resonance Raman Spectra of Bathorhodopsin -- 6.1.3 Fourier Transform Infrared Studies of the Activation Mechanism of Rhodopsin -- 6.1.3.1 Low-temperature Photoproducts -- 6.1.3.2 The Active State Metarhodopsin II (MII) -- 6.2 Infrared Studies of the Light-driven Proton Pump Bacteriorhodopsin -- 6.3 Study of the Anion Uptake by the Retinal Protein Halorhodopsin Using ATR Infrared Spectroscopy -- 6.4 Infrared Studies Using Caged Compounds as the Trigger Source -- References -- 7 Heme Proteins -- 7.1 Vibrational Spectroscopy of Metalloporphyrins -- 7.1.1 Metalloporphyrins Under D(4h) Symmetry -- 7.1.2 Symmetry Lowering -- 7.1.3 Axial Ligation -- 7.1.4 Normal Mode Analyses -- 7.1.5 Empirical Structure-Spectra Relationships -- 7.2 Hemoglobin and Myoglobin -- 7.2.1 Vibrational Analysis of the Heme Cofactor -- 7.2.2 Iron-Ligand and Internal Ligand Modes -- 7.2.3 Probing Quaternary Structure Changes -- 7.3 Cytochrome c - a Soluble Electron-transferring Protein -- 7.3.1 Vibrational Assignments -- 7.3.2 Redox Equilibria in Solution -- 7.3.3 Conformational Equilibria and Dynamics -- 7.3.4 Redox and Conformational Equilibria in the Immobilised State -- 7.3.5 Electron Transfer Dynamics and Mechanism -- 7.3.6 The Relevance of Surface-enhanced Vibrational Spectroscopic Studies for Elucidating Biological Functions -- 7.4 Cytochrome c Oxidase -- 7.4.1 Resonance Raman Spectroscopy -- 7.4.2 Redox Transitions -- 7.4.3 Catalytic Cycle -- 7.4.4 Oxidases from Extremophiles and Archaea -- References -- 8 Non-heme Metalloproteins -- 8.1 Copper Proteins -- 8.2 Iron-Sulfur Proteins -- 8.3 Di-iron Proteins -- 8.4 Hydrogenases -- References -- Subject Index.