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Vibrational spectroscopy techniques, which have traditionally been used to provide non-destructive, rapid, and relevant information on microbial systematics, are useful for classification and identification. In conjunction with advanced chemometrics, infrared spectroscopy enables the biochemical signatures from microbiological structures to be extracted and analysed. In addition, a number of recent studies have shown that Fourier Transform Infrared (FT-IR) spectroscopy can help to understand the molecular basis of events, such as the adaptive tolerance responses expressed by bacteria when exposed to stress conditions in the environment, i.e. environments that cells confront in food and during food processing. The proposed Brief will discuss the published experimental techniques, data-processing algorithms, and approaches used in FT-IR spectroscopy to assist in the characterization and identification of microorganisms, to assess the mechanisms of bacterial inactivation by food processing technologies and antimicrobial compounds, to monitor the spore and membrane properties of foodborne pathogens in changing environments, to detect stress-injured microorganisms in food-related environments, to assess dynamic changes in bacterial populations, and to study bacterial tolerance responses.

Food -- Shelf-life dating. --- Food --- Fourier transform infrared spectroscopy --- Infrared spectroscopy --- Biology --- Health & Biological Sciences --- Biomedical Engineering --- Microbiology & Immunology --- Microbiology --- Fourier transform infrared spectroscopy. --- Infrared spectroscopy. --- Microbiology. --- Infra-red spectrometry --- Infrared spectrometry --- Spectrometry, Infrared --- Spectroscopy, Infrared --- FTIR spectroscopy --- Bacteriology --- Chemistry. --- Spectroscopy. --- Food Science. --- Spectroscopy/Spectrometry. --- Applied Microbiology. --- Biotechnology. --- Optical spectroscopy --- Fourier transform spectroscopy --- Sanitary microbiology --- Food science. --- Microbial biology --- Microorganisms --- Analysis, Spectrum --- Spectra --- Spectrochemical analysis --- Spectrochemistry --- Spectroscopy --- Chemistry, Analytic --- Interferometry --- Optics --- Radiation --- Wave-motion, Theory of --- Absorption spectra --- Light --- Spectroscope --- Science --- Qualitative --- Spectrometry --- Food—Biotechnology. --- Analytical chemistry

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Infrared spectroscopy is a new and innovative technology to study protein folding/misfolding events in the broad arsenal of techniques conventionally used in this field. The progress in understanding protein folding and misfolding is primarily due to the development of biophysical methods which permit to probe conformational changes with high kinetic and structural resolution. The most commonly used approaches rely on rapid mixing methods to initiate the folding event via a sudden change in solvent conditions. Traditionally, techniques such as fluorescence, circular dichroism or visible absorption are applied to probe the process. In contrast to these techniques, infrared spectroscopy came into play only very recently, and the progress made in this field up to date which now permits to probe folding events over the time scale from picoseconds to minutes has not yet been discussed in a book. The aim of this book is to provide an overview of the developments as seen by some of the main contributors to the field. The chapters are not intended to give exhaustive reviews of the literature but, instead to illustrate examples demonstrating the sort of information, which infrared techniques can provide and how this information can be extracted from the experimental data. By discussing the strengths and limitations of the infrared approaches for the investigation of folding and misfolding mechanisms this book helps the reader to evaluate whether a particular system is appropriate for studies by infrared spectroscopy and which specific advantages the techniques offer to solve specific problems.

Biochemistry. --- Infrared spectroscopy. --- Protein folding. --- Proteins -- Analysis. --- Protein folding --- Proteins --- Infrared spectroscopy --- Biochemistry --- Biophysical Processes --- Spectrophotometry --- Biochemical Processes --- Biochemical Phenomena --- Biophysical Phenomena --- Spectrum Analysis --- Physical Processes --- Photometry --- Chemical Processes --- Physical Phenomena --- Chemistry Techniques, Analytical --- Chemical Phenomena --- Investigative Techniques --- Phenomena and Processes --- Analytical, Diagnostic and Therapeutic Techniques and Equipment --- Protein Folding --- Spectrophotometry, Infrared --- Biology --- Human Anatomy & Physiology --- Health & Biological Sciences --- Animal Biochemistry --- Biophysics --- Analysis --- Folding of proteins --- Folding --- Physics. --- Proteins. --- Atomic structure. --- Molecular structure. --- Spectra. --- Biophysics. --- Biological physics. --- Biomaterials. --- Biophysics and Biological Physics. --- Protein Structure. --- Atomic/Molecular Structure and Spectra. --- Conformation --- Biological and Medical Physics, Biophysics. --- Biocompatible materials --- Biomaterials --- Medical materials --- Medicine --- Biomedical engineering --- Materials --- Biocompatibility --- Prosthesis --- Biological chemistry --- Chemical composition of organisms --- Organisms --- Physiological chemistry --- Chemistry --- Medical sciences --- Composition --- Proteins . --- Atomic structure  . --- Molecular structure . --- Bioartificial materials --- Hemocompatible materials --- Structure, Molecular --- Chemical structure --- Structural bioinformatics --- Structure, Atomic --- Atomic theory --- Proteids --- Biomolecules --- Polypeptides --- Proteomics --- Biological physics --- Physics --- Biomaterials (Biomedical materials)