000			03946cam a22004214a 4500
999			_c106278 _d106278
001			14427330
003			OSt
005			20210524114434.0
008			060623s2007 ne a b 001 0 eng
010			_a 2006021096
016	7		_a101280048 _2DNLM
020			_a9780121644918 (alk. paper)
035			_a(OCoLC)ocm70218044
040			_aDNLM/DLC _cDLC
042			_apcc
060	0	0	_a2007 I-373
060	1	0	_aQD 96.N8 _bP967 2007
082	0	0	_a572.636 CAV _222
245	0	0	_aProtein NMR spectroscopy : _bprinciples and practice / _cJohn Cavanagh ... [et al.].
250			_a2nd ed.
260			_aAmsterdam ; _aBoston : _bAcademic Press, _bElsevier, _cc2007.
300			_axxv, 885 p. : _bill. ; _c24 cm.; Hard Bound
500			_a$121.00 TB/236/210720
504			_aIncludes bibliographical references (p. 839-840) and index.
505			_a1. 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 <sup>1</sup>H 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.
520			_a 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
650		0	_aProteins _xAnalysis _vLaboratory manuals.
650		0	_aNuclear magnetic resonance spectroscopy _vLaboratory manuals.
650	1	2	_aMagnetic Resonance Spectroscopy _xmethods.
650	1	2	_aProteins _xanalysis.
700	1		_aCavanagh, John, _d1963-
856	4	1	_3Table of contents only _uhttp://www.loc.gov/catdir/toc/ecip0616/2006021096.html
856	4	2	_3Publisher description _uhttp://www.loc.gov/catdir/enhancements/fy0664/2006021096-d.html
856	4	1	_zAvailable to Stanford-affiliated users at: _uhttp://www.sciencedirect.com/science/book/9780121644918
906			_a7 _bcbc _corignew _d1 _eecip _f20 _gy-gencatlg
942			_2ddc _cBK