Bibliothèque de L'IMIST/CNRST

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Fundamental physics for probing and imaging par Allison, Wade. Publication : [S.l.] Oxford University Press, USA 2006 . 352 p. , This book addresses the question 'What is physics for?' Physics has provided many answers for mankind by extending his ability to see. Modern technology has enabled the power of physics to see into objects to be used in archaeology, medicine including therapy, geophysics, forensics and other spheres important to the good of society. The book looks at the fundamental physics of the various methods and how they are used by technology. These methods are magnetic resonance, ionising radiation and sound. By taking a broad view over the whole field it encourages comparisons, but also addresses questions of risk and benefit to society from a fundamental viewpoint. This textbook has developed from a course given to third year students at Oxford and is written so that it can be used coherently as a basis for shortened courses by omitting a number of chapters. 25 cm. Date : 2006 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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Optical spectroscopy of inorganic solids / par Henderson,, Brian. Publication : [S.l.] : Oxford University Press, 2006 . 672 p. ; , Broché. 24 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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