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Protein NMR spectroscopyprinciples a...

Cavanagh, John, (1963-)

Protein NMR spectroscopyprinciples and practice /

紀錄類型:	書目-電子資源 : Monograph/item
正題名/作者:	Protein NMR spectroscopyJohn Cavanagh ... [et al.].
其他題名:	principles and practice /
其他作者:	Cavanagh, John,
出版者:	Amsterdam ;Academic Press,c2007.
面頁冊數:	xxv, 885 p. :ill. ;24 cm.
標題:	ProteinsCongresses.Analysis
電子資源:	An electronic book accessible through the World Wide Web; click for information
ISBN:	9780121644918

Protein NMR spectroscopyprinciples and practice /
Protein NMR spectroscopyprinciples and practice /[electronic resource] :John Cavanagh ... [et al.]. - 2nd ed. - Amsterdam ;Academic Press,c2007. - xxv, 885 p. :ill. ;24 cm.

Includes bibliographical references (p. 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 <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.

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.

Electronic reproduction.
Amsterdam :
Elsevier Science & Technology,
2007.

Mode of access: World Wide Web.

ISBN: 9780121644918

Source: 89676:89676Elsevier Science & Technologyhttp://www.sciencedirect.comSubjects--Topical Terms:

439993
Proteins
--Analysis--Congresses.Index Terms--Genre/Form:

214472
Electronic books.

LC Class. No.: QP551 / .P69726 2007eb

Dewey Class. No.: 572/.636

National Library of Medicine Call No.: QD 96.N8 / P967 2007

Protein NMR spectroscopyprinciples and practice /
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300 $a xxv, 885 p. : $b ill. ; $c 24 cm.
504 $a Includes bibliographical references (p. 839-840) and index.
505 0 $a 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 <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.
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