TY - BOOK AU - Cavanagh,John TI - Protein NMR spectroscopy: principles and practice SN - 9780121644918 AV - QP551 .P69726 2007eb U1 - 572/.636 22 PY - 2007/// CY - Amsterdam, Boston PB - Academic Press KW - Proteins KW - Analysis KW - Laboratory manuals KW - Nuclear magnetic resonance spectroscopy KW - Magnetic Resonance Spectroscopy KW - methods KW - analysis KW - Prot�eines KW - Analyse KW - Manuels de laboratoire KW - Spectroscopie de la r�esonance magn�etique nucl�eaire KW - SCIENCE KW - Life Sciences KW - Biochemistry KW - bisacsh KW - fast KW - Chemische Analyse KW - gnd KW - NMR-Spektroskopie KW - Proteine KW - NMR KW - gtt KW - Eiwitten KW - Theorie KW - Magnetische relaxatie KW - Dynamica KW - Electronic books KW - lcgft N1 - Includes bibliographical references (pages 839-840) and index; Preliminary Table of Contents -- 1. Classical NMR Spectroscopy -- 2. Theoretical Description of NMR Spectroscopy -- 3. Experimental Aspects of NMR Spectroscopy -- 4. Multi-Dimensional NMR Spectroscopy -- 5. Relaxation and Dynamic Processes -- 6. Experimental 1H NMR Methods -- 7. Heteronuclear NMR Experiments -- 8. Experimental NMR Relaxation Methods -- 9. Larger Proteins and Molecular Interactions -- 10. Sequential Assignment, Structure Determination and Other Applications N2 - 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 UR - https://www.sciencedirect.com/science/book/9780121644918 ER -