3 edition of NMR spectroscopy of biological solids found in the catalog.
NMR spectroscopy of biological solids
|Statement||edited by A. Ramamoorthy.|
|The Physical Object|
|Pagination||353 p. :|
|Number of Pages||353|
Magnetic Resonance Spectroscopy is a unique tool to probe the biochemistry in vivo providing metabolic information non-invasively. In this book, topics of MRS both relevant to the clinic and also those that are beyond the clinical arena are covered. The book consists of two sections. This book presents a critical assessment of progress on the use of nuclear magnetic resonance spectroscopy to determine the structure of proteins, including brief reviews of the history of the field along with coverage of current clinical and in vivo applications. The book, in honor of Oleg Price: $
Summary. NMR Spectroscopy in Liquids and Solids provides an introduction of the general concepts behind Nuclear Magnetic Resonance (NMR) and its applications, including how to perform adequate NMR experiments and interpret data collected in liquids and solids to characterize molecule systems in terms of their structure and dynamics.. The book is composed of ten chapters. Noté /5. Retrouvez NMR Spectroscopy of Biological Solids et des millions de livres en stock sur Achetez neuf ou d'occasionFormat: Relié.
Abstract. Proton NMR spectroscopy of solids has traditionally been challenging due to the widespread presence of strong 1 H-1 H dipolar couplings in solid systems, which severely broaden proton NMR spectral lines and result in the loss of chemical resolution. Nonetheless, recent developments in magic-angle-spinning (MAS) NMR probe technology and solid-state NMR . Solid-state nuclear magnetic resonance (NMR) spectroscopy is at this time well-established as a valuable technique for characterizing a variety of polymer systems. A multitude of NMR experiments can be used to gain valuable practical information about the molecular structure, conformation, and dynamics of polymer chains in various polymer : Antonio Martínez-Richa, Regan L. Silvestri.
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Filling a void in the current literature, NMR Spectroscopy of Biological Solids examines all the recent developments, implementation, and interpretation of solid-state NMR experiments and the advantages of applying them to biological systems. The book emphasizes how these techniques can be used to realize the structure of non-crystalline systems of any : Hardcover.
Filling a void in the current literature, NMR Spectroscopy of Biological Solids examines all the recent developments, implementation, and interpretation of solid-state NMR experiments and the advantages of applying them to biological systems.
The book emphasizes how these techniques can be used to realize the structure of non-crystalline systems of any size. Over the past decade, a myriad of techniques have shown that solid-state nuclear magnetic resonance (NMR) can be used in a broad spectrum of Cited by: NMR Spectroscopy of Biological Solids - CRC Press Book Over the past decade, a myriad of techniques have shown that solid-state nuclear magnetic resonance (NMR) can be used in a broad spectrum of applications with exceptionally impressive results.
This book presents a critical assessment of progress on the use of nuclear magnetic resonance spectroscopy to determine the structure of proteins, including brief reviews of the history of the field along with coverage of current clinical and in vivo applications.
The book is a unique mix of NMR methods and biological applications which makes it a convenient reference for those interested in research in this interdisciplinary area of physics, chemistry, biology, and medicine.
This book is intended to provide an in-depth understanding of 13C NMR as a tool in biological research. A method for correlating resonance frequencies in groups of NMR active nuclei based upon a shared J-coupling (indirect spin-spin or scalar-coupling) interaction for the purpose of uniquely assigning nuclear magnetic resonance frequencies to specific backbone and side chain atoms in a solid-state protein.
Solid-state NMR results can yield high-resolution details on the structure and function of many important biological solids, including viruses, fibril-forming molecules, and molecules embedded in the cell membrane.
Filling a void in the current literature, NMR Spectroscopy. Solid state NMR is rapidly emerging as a universally applicable method for the characterization of ordered structures that cannot be studied with solution methods or diffraction techniques.
This proceedings -; from a recent international workshop - captures an image of the latest developments. NMR Spectroscopy in Liquids and Solids provides an introduction of the general concepts behind Nuclear Magnetic Resonance (NMR) and its appli- cations, including how to perform adequate NMR experiments and interpret data collected in liquids and solids to characterize molecule systems in terms.
About this book. The complexity and heterogeneity of biological systems has posed an immense challenge in recent years. An increasingly important tool for obtaining molecular and atomic scale information on a range of large biological molecules and cellular components is solid state NMR.
Introduction to Solid-State NMR Spectroscopy. Analysis of Pulse Sequences Using Computer Simulations. Measurement of NMR Parameters from Aligned Biological Solids. Filling a void in the current literature, NMR Spectroscopy of Biological Solids expounds on all the pertinent and up-to-date information regarding Addressing principles, methods, and applications, it considers how solid-state NMR is being employed to solve a wide range of practical problems that arise in both academic and industrial research.
The book covers two-dimensional, three-dimensional, and four-dimensional NMR, and their application to protein and DNA structure determination. A unique feature is the coverage of the biological aspects of solid-state NMR spectroscopy.
From the reviews: "This book surveys much of the current research in the area of biological solid-state NMR spectroscopy, and as such should be of great interest to the chemical, biochemical, and biophysical communities.
and T. Gullion, Structural Determination of Biological Solids by Magic-Angle Spinning 13C NMR. J.A. Hamilton, 13C NMR Studies of the Interactions of Fatty Acids with Phospholipid Bilayers, Plasma Lipoproteins, and Proteins.
Konnecke, Application 13C NMR Spectroscopy to Metabolic Studies on Animals. Solid-state MHz ( T) NMR spectrometer at the Canadian National Ultrahigh-field NMR Facility for Solids Solid-state NMR (ssNMR) spectroscopy is a special type of nuclear magnetic resonance (NMR) spectroscopy, characterized by the presence of anisotropic (directionally dependent) interactions.
The proton chemical shift (CS) tensor is a sensitive probe of structure and hydrogen bonding. Highly accurate quantum-chemical protocols exist for computation of 1H magnetic shieldings in the various contexts, making proton chemical shifts potentially a powerful predictor of structural and electronic properties.
However, 1H CS tensors are not yet widely used in protein structure calculation Cited by: Nuclear magnetic resonance (NMR) is a well-established analytical method used for qualitative and quantitative analyses in various areas and applications. It utilizes a phenomenon where nuclei of a certain atom is resonating at a specific secondary oscillating magnetic field under a strong static magnetic field.
Experimental Approaches of NMR Spectroscopy, Methodology and Application to Life Science and Materials Science. The Nuclear Magnetic Resonance Society of Japan (Ed.) Springer, Singapore (). Solid State NMR: Principles, Methods and Applications, Klaus Muller and Marco Geppi.
With additional coverage of the practical implementation of solid-state NMR experiments integrated into the discussion, this book will be essential reading for all those using, or about to use, solid-state NMR spectroscopy. Dr Melinda Duer is a senior lecturer in the Department of Chemistry at the University of Cambridge, Cambridge, : Melinda J.
Duer. NMR spectroscopy is a powerful tool for biologists interested in the structure, dynamics, and interactions of biological macromolecules. This review aims at presenting in an accessible manner the requirements and limitations of this by: The book is divided into two parts: "Fundamentals" and "Further Applications." The section on Fundamentals contains relatively long chapters that deal with the basic theory and practice of solid-state NMR.
The essential differences and extra scope of solid-state NMR over solution-state is dealt with in an introductory chapter.