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In this thesis, two-dimensional infrared spectroscopy (2D-IR) spectroscopy is used to study changes in structure and dynamics in deoxyribonucleic acid (DNA) containing only Adenine-Thymine (AT) base pairs. The aims of the studies in this thesis are to demonstrate the ability of 2D-IR spectroscopy to extract unique dynamic information, not accessible via established experimental methods from nucleic acid systems, as it has for protein- and peptide-based systems. The underlying theory of both linear and nonlinear 2D-IR spectroscopies is described in the initial Chapter, following this the details of the types of information already obtained using these methods from DNA in the current literature is presented.
Temperature-jump (T-jump) two-dimensional infrared spectroscopy (2D IR) is developed, characterized, and applied to the study of protein folding and association. In solution, protein conformational changes span a wide range of timescale from nanoseconds to minutes. Ultrafast 2D IR spectroscopy measures time-dependent structural changes within the protein ensemble by probing the frequency changes associated with amide I backbone vibrations. Combining 2D IR with a perturbing laser-induced T-jump enables the study of conformational dynamics from 5 ns to 50 ms. To access a finer time-sampling of the conformational evolution, a one-dimensional variant of 2D IR, heterodyne-detected dispersed vibrational echo spectroscopy (HDVE), is implemented. The framework for interpreting transient HDVE and 2D IR spectra is developed, and we propose a method to remove the linear absorption distortions along both frequency axes. We first present the T-jump 2D IR spectra of a dipeptide to reveal the general amide I baseline response expected in the absence of conformational change. To facilitate the analysis of T-jump data, singular value decomposition (SVD) is employed for reducing noise, identifying the number of distinguishable states, and separating spectral changes based on shared timescales. Finally, T-jump 2D IR spectroscopy is applied to study the unfolding of ubiquitin, disordering of the 12-residue p-hairpin peptide trpzip2 (TZ2), and the dissociation of insulin dimers to monomers. Experimental results for ubiquitin highlight the importance of linear absorption corrections for interpretation of the data. In response to the T-jump, 2D IR results indicate p-sheet structure melts in ubiquitin with a small amplitude (~10 gs) and large amplitude (17 ms) response. Isotope-labeling T-jump experiments on TZ2 allow for the proposal of a free energy surface in which transitions from a native and misfolded state proceed through a disordered hub-like state with a 1-2 gs timescale. Multiple timescales are observed in the T-jump induced dissociation of insulin. Based on their spectral features and concentration dependence, the insulin timescales can be assigned to dissociation, disordering, and oligomerization processes. With these applications, we demonstrate the capability of T-jump 2D IR spectroscopy to reveal detailed molecular dynamics.
The Encyclopedia of Biophysics is envisioned both as an easily accessible source of information and as an introductory guide to the scientific literature. It includes entries describing both Techniques and Systems. In the Techniques entries, each of the wide range of methods which fall under the heading of Biophysics are explained in detail, together with the value and the limitations of the information each provides. Techniques covered range from diffraction (X-ray, electron and neutron) through a wide range of spectroscopic methods (X-ray, optical, EPR, NMR) to imaging (from electron microscopy to live cell imaging and MRI), as well as computational and simulation approaches. In the Systems entries, biophysical approaches to specific biological systems or problems – from protein and nucleic acid structure to membranes, ion channels and receptors – are described. These sections, which place emphasis on the integration of the different techniques, therefore provide an inroad into Biophysics from a biological more than from a technique-oriented physical/chemical perspective. Thus the Encyclopedia is intended to provide a resource both for biophysicists interested in methods beyond those used in their immediate sub-discipline and for those readers who are approaching biophysics from either a physical or biological background.
Vols. for 1963- include as pt. 2 of the Jan. issue: Medical subject headings.
The book highlights recent developments in the field of spectroscopy by providing the readers with an updated and high-level of overview. The focus of this book is on the introduction to concepts of modern spectroscopic techniques, recent technological innovations in this field, and current examples of applications to molecules and materials relevant for academia and industry. The book will be beneficial to researchers from various branches of science and technology, and is intended to point them to modern techniques, which might be useful for their specific problems. Spectroscopic techniques, that are discussed include, UV-Visible absorption spectroscopy, XPS, Raman spectroscopy, SERS, TERS, CARS, IR absorption spectroscopy, SFG, LIBS, Quantum cascade laser (QCL) spectroscopy, fluorescence spectroscopy, ellipsometry, cavity-enhanced absorption spectroscopy, such as cavity ring-down spectroscopy (CRDS) and evanescent wave-CRDS both in gas and condensed phases, time-resolved spectroscopy etc. Applications introduced in the different chapters demonstrates the usefulness of the spectroscopic techniques for the characterization of fundamental properties of molecules, e.g. in connection with environmental impact, bio-activity, or usefulness for pharmaceutical drugs, and materials important e.g. for nano-science, nuclear chemistry, or bio-applications. The book presents how spectroscopic techniques can help to better understand substances, which have also great impact on questions of social and economic relevance (environment, alternative energy, etc.).
This book embraces all physiochemical aspects of the structure and molecular dynamics of water, focusing on its role in biological objects, e.g. living cells and tissue, and in the formation of functionally active structures of biological molecules and their ensembles. Water is the single most abundant chemical found in all living things. It offers a detailed look into the latest modern physical methods for studying the molecular structure and dynamics of the water and provides a critical analysis of the existing literature data on the properties of water in biological objects. Water as a chemical reagent and as a medium for the formation of conditions for enzymatic catalysis is a core focus of this book. Although well suited for active researchers, the book as a whole, as well as each chapter on its own, can be used as fundamental reference material for graduate and undergraduate students throughout chemistry, physics, biophysics and biomedicine.