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200 and more nmr experiments par Berger,, Stefan. Publication : [S.l.] Wiley-VCH 2004 . 854 p. , This work-book will guide you safely, in step-by-step descriptions, through every detail of the NMR experiments within, beginning with 1D routine experiments and ending with a series of advanced 3D experiments on a protein: ? Which experiment can best yield the desired information? ? How must the chosen experiment be performed? ? How does one read the required information from the spectrum? ? How does this particular pulse sequence work? ? Which other experiments give similar information? This third edition of the book, following its two highly successful predecessors, has been revised and expanded to 206 experiments. They are organized in 15 chapters, covering test procedures and routine spectra, variable temperature measurements, the use of auxiliary reagents, 1D multipulse experiments, spectra of heteronuclides, and the application of selective pulses. The second and third dimensions are introduced using pulsed field gradients, and experiments on solid state materials are described. A key part describes 3D experiments on the protein ubiquitin with 76 amino acids. What is new in this third edition? 1. 24 new experiments have been inserted into the 14 chapters that were in the 2nd edition, e.g., alpha/beta-SELINCOR-TOCSY, WET, DOSY, ct-COSY, HMSC, HSQC with adiabatic pulses, HETLOC. J-resolved HMBC, (1,1)- and (1,n)-ADEQUATE, STD, REDOR, and HR-MAS. 2. 20 new protein NMR experiments have been specially devised and are collected in the newly added Chapter 15, ProteinNMR, for which one needs a special model sample: fully 13C- and 15N-labeled human ubiquitin. Techniques used include the constant time principle, the PEP method, filters, gradient selection, and the echo/anti-echo procedure. The guide has been written by experts in this field, following the principle of learning by doing: all the experiments have been specially performed for this book, exactly as described and shown in the spectra that are reproduced. Being a reference source and work-book for the NMR laboratory as well as a textbook, it is a must for every scientist working with NMR, as well as for students preparing for their laboratory courses. 24 cm. Date : 2004 Disponibilité : Exemplaires disponibles: La bibliothèque des Sciences Exactes et Naturelles (1),

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Advanced applications of nmr to organometallic chemistry   Publication : Chichester ; New York Wiley 1996 . 376 p. , This new series offers leading contributions by well known chemists reviewing the state-of-the-art of this wide research area. Physical Organometallic Chemistry aims to develop new insights and to promote novel interest and investigations applicable to organometallic chemistry. NMR spectroscopy has had a considerable impact on many fields of chemistry, although it has served organometallic chemistry mainly on a routine level. In a collection of reviews, leading chemists provide an insight into the scope of applications and uncover the potential of this technique for organometallic chemists. Advanced Applications of NMR to Organometallic Chemistry; * Illustrates how recent 1D and 2D and specialized multinuclear applications can solve specific problems encountered by organometallic chemists * Surveys modern NMR techniques in organometallic chemistry * Includes metal NMR related techniques * Focuses on the advent of solid state NMR in organometallic chemistry This book will prove invaluable to the NMR spectroscopist and organometallic chemists and will also be of interest to all organic, inorganic and physical chemists Contents: Selective Excitation and Selective Detection in ?29Si NMR; Two-dimensional ?13C, Metal Nuclei Correlation; Two-dimensional ?1H-?119Sn Proton Detected Correlation Spectroscopy in Coordination Chemistry of Hypervalent Organotin Compounds; Indirect Nuclear ?119Sn-X Spin-Spin Coupling; Solid State NMR Applications in Organotin and Organolead Chemistry; Solid State NMR Investigations of Metal Carbonyl Complexes; High Pressure NMR in Organometallic Chemistry; Multinuclear NMR Spectroscopy in Supercritical Fluids; High Resolution ?6,7Li NMR of Organolithium Compounds; Metal NMR of Organovanadium, -Niobium and -Tantalum Compounds; NMR of Metallic Nuclei in Clusters; ?171Yb NMR Spectroscopy. 24 cm. Date : 1996 Disponibilité : Exemplaires disponibles: La bibliothèque des Sciences Exactes et Naturelles (1),

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Essential NMR for scientists and engineers / par BlŁumich,, Bernhard. Publication : Berlin : Springer, 2005 . 243 p. : , "With 110 figures." 15 x 20 cm. Date : 2005 Disponibilité : Exemplaires disponibles: La bibliothèque des Sciences Exactes et Naturelles (1),

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Essential practical NMR for organic chemistry / par Richards, S. A. Publication : Chichester, West Sussex, U.K. : John Wiley, 2011 . 1 online resource (x, 216 pages) : Date : 2011 Disponibilité : Exemplaires disponibles: La bibliothèque des Sciences Exactes et Naturelles (1),

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Fundamentals of protein nmr spectroscopy / par Rule,, Gordon S. Publication : [S.l.] Springer 2005 . 557 p. , NMR spectroscopy has proven to be a powerful technique to study the structure and dynamics of biological macromolecules. Fundamentals of Protein NMR Spectroscopy is a comprehensive textbook that guides the reader from a basic understanding of the phenomenological properties of magnetic resonance to the application and interpretation of modern multi-dimensional NMR experiments on 15N/13C-labeled proteins. Beginning with elementary quantum mechanics, a set of practical rules is presented and used to describe many commonly employed multi-dimensional, multi-nuclear NMR pulse sequences. A modular analysis of NMR pulse sequence building blocks also provides a basis for understanding and developing novel pulse programs. This text not only covers topics from chemical shift assignment to protein structure refinement, as well as the analysis of protein dynamics and chemical kinetics, but also provides a practical guide to many aspects of modern spectrometer hardware, sample preparation, experimental set-up, and data processing. End of chapter exercises are included to emphasize important concepts. Fundamentals of Protein NMR Spectroscopy not only offer students a systematic, in-depth, understanding of modern NMR spectroscopy and its application to biomolecular systems, but will also be a useful reference for the experienced investigator. 25 cm. Date : 2005 Disponibilité : Exemplaires disponibles: La bibliothèque des Sciences Exactes et Naturelles (1),

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In vivo NMR spectroscopy : principles and techniques par Graaf,, Robin A. de. Publication : [S.l.] Wiley-Interscience 2007 . 592 p. , This is the second edition of a unique book in the field of in vivo NMR covering in detail the technical and biophysical aspects of the technique. The contents of the book are appropriate to both beginners and experienced users of in vivo NMR spectroscopy. The new edition is focussed on bringing the reader practical insights and advice, but is also geared towards use as a study aid and in NMR courses. Recent advances in NMR spectroscopy, like high field NMR, hyperpolarized NMR and new localization and editing techniques have been included. An extensive and updated treatment of radiofrequency pulses is given, together with several tables and recipes for their generation. Solutions to the exercises within this text can be found here. 25 cm. Date : 2007 Disponibilité : Exemplaires disponibles: La bibliothèque des Sciences Médicales et Pharmaceutiques (1),

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Organic structure determination using 2-d nmr spectroscopy a problem-based approach par Simpson, Jeffrey H. Publication : [S.l.] Academic Press 2008 . 384 p. , This book contains 30-40 quality 2D NMR data sets following an introductory section describing the methodology employed. Many other books describe the methods used, but none offer a large number of problems. Instructors at universities and colleges at the present time are forced to cobble together problems from a wide range of sources. The fragmentary approach to assembling course materials has a negative impact on course continuity and thus adversely impacts student retention. This book will stand as a single source to which instructors and students can go to obtain a comprehensive compendium of NMR problems of varying difficulty. . Presents strategies for assigning resonances to known structures and for deducing structures of unknown organic molecules based on their NMR spectra . Contains 20 known and 20 unknown structure determination problems . Features a supporting website from which instructors can download the structures of the unknowns in selected chapters, digital versions of all figures, and raw data sets for processing. 24 cm. Date : 2008 Disponibilité : Exemplaires disponibles: La bibliothèque des Sciences Exactes et Naturelles (1),

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Principles of nuclear magnetic resonance microscopy / par Callaghan, Paul T. Publication : Oxford [England] : | New York : Clarendon Press ; | Oxford University Press, 1991 . xvii, 492 p. : 24 cm. Date : 1991 Disponibilité : Exemplaires disponibles: La bibliothèque des Sciences Exactes et Naturelles (1),

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Protein NMR spectroscopy, second edition : principles and practice par Cavanagh,, John. Publication : [S.l.] Academic Press 2006 . 912 p. , Protein NMR Spectroscopy combines a comprehensive theoretical treatment of NMR spectroscopy with an extensive exposition of the experimental techniques applicable to proteins and other biological macromolecules in solution. Beginning with simple theoretical models and experimental techniques, Protein NMR Spectroscopy develops the complete repertoire of theoretical principles and experimental techniques necessary for understanding and implementing the most sophisticated NMR experiments. Important new techniques and applications of NMR spectroscopy have emerged since the first edition of this extremely successful book was published in 1996. The second edition includes new sections describing measurement and use of residual dipolar coupling constants for structure determination, TROSY and deuterium labeling for application to large macromolecules, and experimental techniques for characterizing conformational dynamics. In addition, the treatments of instrumentation and signal acquisition, field gradients, multidimensional spectroscopy, and structure calculation are updated and enhanced. Protein NMR Spectroscopy is written as a graduate-level textbook and will be of interest to biochemists, chemists, biophysicists, and structural biologists who utilize NMR spectroscopy or who wish to understand the latest developments in this field. Provides an understanding of the theoretical principles important for biological NMR spectroscopy Demonstrates how to implement, optimize and troubleshoot modern multi-dimensional NMR experiments Allows for the capability of designing effective experimental protocols for investigations of protein structures and dynamics Includes a comprehensive set of example NMR spectra of ubiquitin provides a reference for validation of experimental methods. 23 cm. Date : 2006 Disponibilité : Exemplaires disponibles: La bibliothèque des Sciences Exactes et Naturelles (1),

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Solid state nmr spectroscopy for biopolymers : principles and applications / par Saitʋ,, Hazime. Publication : [S.l.] : Springer, 2006 . 464 p. ; , When considering the biological significance and industrial and medical applications of biopolymers, it is crucial to know details of their secondary structure, dynamics and assembly. The biopolymers include globular, membrane and fibrous proteins, polypeptides, nucleic acids, polysaccharides and lipids. Solid state NMR spectroscopy has proved to be the most suitable and unrivaled means for investigations of biopolymers. The major advantage of solid state NMR spectroscopy is that the resulting line widths can be manipulated experimentally and are not influenced by motional fluctuation of proteins under consideration as a whole. Solid State NMR Spectroscopy for Biopolymers: Principles and Applications provides a comprehensive account on how the conformation and dynamics of such biopolymers can be revealed by solid state NMR spectroscopy. Special efforts have been made towards the historical and chronological consequences of a variety of applications and the dynamic aspects of the biopolymer system. In particular, the authors emphasise how important it is to record the most simple DD-MAS (one pulse excitation with high power decoupling) as a mean of locating very flexible portions of membrane proteins and membrane associated peptides. The authors also demonstrate that dynamic features of membrane proteins with a timescale of fast (10 8 Hz) and intermediate (10 4 -10 5 Hz) fluctuation motions can be revealed easily by specific suppression of peaks. 25 cm. Date : 2006 Disponibilité : Exemplaires disponibles: La bibliothèque des Sciences Exactes et Naturelles (1),

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