Far Infrared Spectroscopy of Biomolecules and Water PDF Download

Author: Syed Khadim Husain
Publisher:
ISBN:
Category :
Languages : en
Pages : 664

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Author: Henry H. Mantsch
Publisher: Wiley-Liss
ISBN:
Category : Science
Languages : en
Pages : 384

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Book Description
Infrared Spectroscopy of Biomolecules Edited by Henry H. Mantsch and Dennis Chapman Dramatic new advances in the application of infrared spectroscopy to biomolecules and instrumentation are revolutionizing this branch of molecular spectroscopy. Infrared Spectroscopy of Biomolecules provides an up-to-date, detailed look at the different spectroscopic techniques now available and offers a framework for progression in the field, including the evolution of Fourier transform methods, the development of time-resolved techniques and difference spectroscopy, as well as new modulation methods. The book begins with a fundamental introduction to the theories behind both infrared spectroscopy and the Fourier transform method, which lays the groundwork for the instrumental and mathematical chapters that follow. Once the basics of the infrared methods are established, the proceeding chapters cover the application of infrared spectroscopy to proteins, lipids, enzymes, nucleic acids, carbohydrates, and biomembranes. Other chapters in this excellent reference include: Theoretical Analyses of the Amide I Infrared Bands of Globular Proteins Slow and Fast Infrared Kinetic Studies Fourier Transform Infrared Spectroscopy of Cell Surface Polysaccharides What Can Infrared Spectroscopy Tell Us About the Structure and Composition of Intact Bacterial Cells Biomedical Infrared Spectroscopy Editors Henry Mantsch and Dennis Chapman, leading experts in the field, conclude with an exciting look at much-anticipated future developments, including the use of caged compounds and studies of oxidation reduction systems within the IR spectrometer. A solid introduction to the basics with up-to-the-minute coverage of the latest developments in the field, Infrared Spectroscopy of Biomolecules is an indispensable reference tool for biochemists, biophysicists, and structural biologists alike.

Author: Camille Sandorfy
Publisher: Springer Science & Business Media
ISBN: 9400964900
Category : Science
Languages : en
Pages : 639

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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: A. Barth
Publisher: IOS Press
ISBN: 160750457X
Category : Medical
Languages : en
Pages : 448

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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: Hans-Ulrich Gremlich
Publisher: CRC Press
ISBN: 9780824704094
Category : Science
Languages : en
Pages : 604

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Book Description
Infrared and Raman Spectroscopy of Biological Materials facilitates a comprehensive and through understanding of the latest developments in vibrational spectroscopy. It contains explains key breakthroughs in the methodologies and techniques for infrared, near-infrared, and Raman spectroscopy. Topics include qualitative and quantitative analysis, biomedical applications, vibrational studies of enzymatic catalysis, and chemometrics.

Author: Roger L. Lundblad
Publisher: CRC Press
ISBN: 1351680544
Category : Medical
Languages : en
Pages : 412

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Book Description
This book is an accessible resource offering practical information not found in more database-oriented resources. The first chapter lists acronyms with definitions, and a glossary of terms and subjects used in biochemistry, molecular biology, biotechnology, proteomics, genomics, and systems biology. There follows chapters on chemicals employed in biochemistry and molecular biology, complete with properties and structure drawings. Researchers will find this book to be a valuable tool that will save them time, as well as provide essential links to the roots of their science. Key selling features: Contains an extensive list of commonly used acronyms with definitions Offers a highly readable glossary for systems and techniques Provides comprehensive information for the validation of biotechnology assays and manufacturing processes Includes a list of Log P values, water solubility, and molecular weight for selected chemicals Gives a detailed listing of protease inhibitors and cocktails, as well as a list of buffers

Author: René Costard
Publisher: Springer
ISBN: 3319220667
Category : Science
Languages : en
Pages : 112

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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: Jeffrey T. Shattuck
Publisher:
ISBN:
Category :
Languages : en
Pages : 306

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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: Theophanides Theophile
Publisher: BoD – Books on Demand
ISBN: 9535117378
Category : Science
Languages : en
Pages : 175

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Book Description
This informative and state-of-the-art book on Infrared Spectroscopy is addressed to Researchers in Medicine as well as to Pharmaceutical Industry and Agriculture. It features 7 specialized chapters of MIRS and NIRS covering applications in proteins and biopolymers; food quality research and food safety applications; and medical applications, such as Down syndrome disorders of tooth, probing of brain oxygen, the role of CO2 in blood pressure and diagnosis of metastatic cancer. This book highlights the span of modern Infrared applications.

Author: C.-M. Pradier
Publisher: Elsevier
ISBN: 0444535594
Category : Science
Languages : en
Pages : 344

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Book Description
IR spectroscopy has become without any doubt a key technique to answer questions raised when studying the interaction of proteins or peptides with solid surfaces for a fundamental point of view as well as for technological applications. Principle, experimental set ups, parameters and interpretation rules of several advanced IR-based techniques; application to biointerface characterisation through the presentation of recent examples, will be given in this book. It will describe how to characterise amino acids, protein or bacterial strain interactions with metal and oxide surfaces, by using infrared spectroscopy, in vacuum, in the air or in an aqueous medium. Results will highlight the performances and perspectives of the technique. Description of the principles, expermental setups and parameter interpretation, and the theory for several advanced IR-based techniques for interface characterisation Contains examples which demonstrate the capacity, potential and limits of the IR techniques Helps finding the most adequate mode of analysis Contains examples Contains a glossary by techniques and by keywords