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Author: Jeffrey T. Shattuck Publisher: ISBN: Category : Languages : en Pages : 306
Book Description
Abstract: Ultrafast infrared pump-probe and photon echo spectroscopy is used to provide insight into the differences of the hydrogen bonding network of water in neat liquid, aqueous solutions and lipid membrane environments. Due to water's fundamental role in biology and biological processes, it is essential to understand its interactions with these environments.The vibrational energy relaxation (VER) mechanism of the libration-bend combination band of neat water was investigated using pump-probe spectroscopy. Previous studies concentrate on the kinetics stretch and bend normal modes. Two concerted pathways were needed to describe the energy relaxation. In the first pathway vibrational energy leaves the excited combination band directly (140 fs) populating low frequency modes. In the second pathway the combination band decays to the bend normal mode which subsequently relaxes to librations and finally to low frequency modes (840 fs).Pump-probe spectroscopy was used to determine perturbations to the VER of nitrous oxide (N2 O) dissolved in water caused by ionic solutes and membranes. Altering the cation for a number of chloride salts showed the VER rate of N2 O to follow a Hofmeister series trend. Kosmotropes Ca2+ , and Mg2+ , increased the lifetime of the u 3 mode of N2 O while chaotropes (Cs+ ) decreased the lifetime. The u3 lifetime of N2 O also showed that charged lipid headgroups alter the hydrogen bonding network of interlamellar water. The u3 lifetime of N2 O dissolved in oriented water near the lipid headgroups was 20 ps and changed by over a factor of two compared to its bulk value of 9 ps. Both experiments show that strongly oriented water slows the N2 O VER by changing the bulk water structure of the intramolecular hydrogen bonding network.Homodyne photon echoes of N2 O in water and octanol, both model environments for head and tail portions of lipids, showed the timescales of spectral diffusion for each solvent. Spectral diffusion timescales for N 2 O in water is caused by inertial rotational motions, 130 fs, and hydrogen bond breaking, 1.5 ps. In octanol spectral diffusion is due to inertial rotation (230 fs), hydrogen bond breaking (3.5 ps), and solvent reorientation (35 ps). Anisotropy measurements are consistent with this interpretation.
Author: Jeffrey T. Shattuck Publisher: ISBN: Category : Languages : en Pages : 306
Book Description
Abstract: Ultrafast infrared pump-probe and photon echo spectroscopy is used to provide insight into the differences of the hydrogen bonding network of water in neat liquid, aqueous solutions and lipid membrane environments. Due to water's fundamental role in biology and biological processes, it is essential to understand its interactions with these environments.The vibrational energy relaxation (VER) mechanism of the libration-bend combination band of neat water was investigated using pump-probe spectroscopy. Previous studies concentrate on the kinetics stretch and bend normal modes. Two concerted pathways were needed to describe the energy relaxation. In the first pathway vibrational energy leaves the excited combination band directly (140 fs) populating low frequency modes. In the second pathway the combination band decays to the bend normal mode which subsequently relaxes to librations and finally to low frequency modes (840 fs).Pump-probe spectroscopy was used to determine perturbations to the VER of nitrous oxide (N2 O) dissolved in water caused by ionic solutes and membranes. Altering the cation for a number of chloride salts showed the VER rate of N2 O to follow a Hofmeister series trend. Kosmotropes Ca2+ , and Mg2+ , increased the lifetime of the u 3 mode of N2 O while chaotropes (Cs+ ) decreased the lifetime. The u3 lifetime of N2 O also showed that charged lipid headgroups alter the hydrogen bonding network of interlamellar water. The u3 lifetime of N2 O dissolved in oriented water near the lipid headgroups was 20 ps and changed by over a factor of two compared to its bulk value of 9 ps. Both experiments show that strongly oriented water slows the N2 O VER by changing the bulk water structure of the intramolecular hydrogen bonding network.Homodyne photon echoes of N2 O in water and octanol, both model environments for head and tail portions of lipids, showed the timescales of spectral diffusion for each solvent. Spectral diffusion timescales for N 2 O in water is caused by inertial rotational motions, 130 fs, and hydrogen bond breaking, 1.5 ps. In octanol spectral diffusion is due to inertial rotation (230 fs), hydrogen bond breaking (3.5 ps), and solvent reorientation (35 ps). Anisotropy measurements are consistent with this interpretation.
Book Description
This thesis presents a highly innovative study of the ultrafast structural and vibrational dynamics of hydrated phospholipids, the basic constituents of cell membranes. As a novel approach to the water-phospholipid interface, the author studies phosphate vibrations using the most advanced methods of nonlinear vibrational spectroscopy, including femtosecond two-dimensional infrared spectroscopy. He shows for the first time that the structure of interfacial water undergoes very limited fluctuations on a 300 fs time scale and that the lifetimes of hydrogen bonds with the phospholipid are typically longer than 10 ps. Such properties originate from the steric hindrance of water fluctuations at the interface and the orienting action of strong electric fields from the phospholipid head group dipoles. In an extensive series of additional experiments, the vibrational lifetimes of the different vibrations and the processes of energy dissipation are elucidated in detail.
Author: A. Barth Publisher: IOS Press ISBN: 160750457X Category : Medical Languages : en Pages : 448
Book Description
Although infrared spectroscopy has been applied with success to the study of important biological and biomedical processes for many years, key advances in this vibrant technique have led to its increasing use, ranging from characterisation of individual macromolecules (DNA, RNA, lipids, proteins) to human tissues, cells and their components. Infrared spectroscopy thus has a significant role to play in the analysis of the vast number of genes and proteins being identified by the various genomic sequencing projects. Whilst this book gives an overview of the field it highlights more recent developments, such as the use of bright synchrotron radiation for recording infrared spectra, the development of two-dimensional infrared spectroscopy and the ability to record infrared spectra at ultrafast speeds. The main focus is on the mid-infrared region, since the great majority of studies are carried out in this region but there is increasing use of the near infrared for biomedical applications and a chapter is devoted to this part of the spectrum. Major advances in theoretical analysis have also enabled better interpretation of the infrared spectra of biological molecules and these are covered. The editors, Professor Andreas Barth of Stockholm University, Stockholm, Sweden and Dr Parvez I. Haris of De Montfort University, Leicester, U.K., who both have extensive research experience in biological infrared spectroscopy per se and in its use in the solution of biophysical problems, have felt it timely therefore to bring together this book. The book is intended for use both by research scientists already active in the use of biological infrared spectroscopy and for those coming new to the technique. Graduate students will also find it useful as an introduction to the technique.
Author: Michael D. Fayer Publisher: CRC Press ISBN: 1466510137 Category : Science Languages : en Pages : 491
Book Description
The advent of laser-based sources of ultrafast infrared pulses has extended the study of very fast molecular dynamics to the observation of processes manifested through their effects on the vibrations of molecules. In addition, non-linear infrared spectroscopic techniques make it possible to examine intra- and intermolecular interactions and how such interactions evolve on very fast time scales, but also in some instances on very slow time scales. Ultrafast Infrared Vibrational Spectroscopy is an advanced overview of the field of ultrafast infrared vibrational spectroscopy based on the scientific research of the leading figures in the field. The book discusses experimental and theoretical topics reflecting the latest accomplishments and understanding of ultrafast infrared vibrational spectroscopy. Each chapter provides background, details of methods, and explication of a topic of current research interest. Experimental and theoretical studies cover topics as diverse as the dynamics of water and the dynamics and structure of biological molecules. Methods covered include vibrational echo chemical exchange spectroscopy, IR-Raman spectroscopy, time resolved sum frequency generation, and 2D IR spectroscopy. Edited by a recognized leader in the field and with contributions from top researchers, including experimentalists and theoreticians, this book presents the latest research methods and results. It will serve as an excellent resource for those new to the field, experts in the field, and individuals who want to gain an understanding of particular methods and research topics.
Book Description
This thesis presents a highly innovative study of the ultrafast structural and vibrational dynamics of hydrated phospholipids, the basic constituents of cell membranes. As a novel approach to the water-phospholipid interface, the author studies phosphate vibrations using the most advanced methods of nonlinear vibrational spectroscopy, including femtosecond two-dimensional infrared spectroscopy. He shows for the first time that the structure of interfacial water undergoes very limited fluctuations on a 300 fs time scale and that the lifetimes of hydrogen bonds with the phospholipid are typically longer than 10 ps. Such properties originate from the steric hindrance of water fluctuations at the interface and the orienting action of strong electric fields from the phospholipid head group dipoles. In an extensive series of additional experiments, the vibrational lifetimes of the different vibrations and the processes of energy dissipation are elucidated in detail.
Author: Gertz I. Likhtenshtein Publisher: Springer Nature ISBN: 3030825035 Category : Science Languages : en Pages : 523
Book Description
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.
Author: Camille Sandorfy Publisher: Springer Science & Business Media ISBN: 9400964900 Category : Science Languages : en Pages : 639
Book Description
This volume contains the proceedings of the NATO-Advanced Study Institute on the "Spectroscopy of Biological Molecules", which took place on July 4-15, 1983 in Acquafredda di Maratea, Italy. The institute concentrated on three main subiects: the structure and dymanics of DNA, proteins, and visual and plant pigments. Its timeliness has been linked to rapid advances in certain spectroscopic techniques which yielded a consider able amount of new information on the structure and inter actions of biologically important molecules. Among these techniques Fourier transform infrared, resonance and surface enhanced 'Raman spectroscopies, Raman microscopy and micro probing, time resolved techniques, two photon and ultrafast electronic, and C-13, N-15 and P-31 NMR spectroscopies and kinetic and static IR difference spectroscopy receiced a great deal of attention at the Institute. In addition, an entirely new technique, near-millimeter-wave spectroscopy has been presented and discussed. Two introductory quantum chemical lectures, one on the structure of water in DNA, and another pn the energy bands in DNA and proteins set the stage for the experimentally oriented lectures that followed. Fundamental knowledge on hydrogen bonding was the topic of two other lectures. Panel discussions were held on the structure and confor mations of DNA, metal-DNA adducts and proteins and on visual pigments. Many scientists who normally attend different conferences and never meet, met at Aquafredda di Maratea. We feel, that at the end of our Institute a synthetic vi~w emerged on the powerful spectroscopic and theoretical methods which are now available for the study of biological molecules.
Author: Frank Parker Publisher: Springer Science & Business Media ISBN: 1468418726 Category : Science Languages : en Pages : 612
Book Description
This book is not intended to be a basic text in infrared spectroscopy. Many such books exist and I have referred to them in the text. Rather, I have tried to find applications that would be interesting to a variety of people: advanced undergraduate chemistry students, graduate students and research workers in several disciplines, spectros copists, and physicians active in research or in the practice of medicine. With this aim in mind there was no intent to have exhaustive coverage of the literature. I should like to acknowledge my use of several books and reviews, which were invaluable in my search for material: G. H. Beaven, E. A. Johnson, H. A. Willis and R. G. 1. Miller, Molecular Spec troscopy, Heywood and Company, Ltd., London, 1961. J. A. Schell man and Charlotte Schellman, 'The Conformation of Polypeptide Chains in Proteins," in The Proteins, Vol. II, 2nd Ed. (H. Neurath, ed.), Academic Press, New York, 1964. R. T. O'Connor, "Application of Infrared Spectrophotometry to Fatty Acid Derivatives," J. Am. Oil Chemists' Soc. 33, 1 (1956). F. L. Kauffman, "Infrared Spectroscopy of Fats and Oils," J. Am. Oil Chemists' Soc. 41,4 (1964). W. J. Potts, Jr., Chemical Infrared Spectroscopy, Vol. I, Techniques, Wiley, New York, 1963. R. S. Tipson, Infrared Spectroscopy of Carbohydrates, National Bureau of Standards Monograph llO, Washington, D.C., 1968. C. N. R. Rao, Chemical Applications of Infrared Spectroscopy, Academic Press, New York, 1963.
Author: Jeffrey T. Shattuck
Author: Jeffrey T. Shattuck
Author: René Costard
Author: A. Barth
Author: Michael D. Fayer
Author: Avishek Ghosh
Author: René Costard
Author: Gertz I. Likhtenshtein
Author: Hector L. Casal
Author: Camille Sandorfy
Author: Frank Parker