Overview
- Editors:
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A. Kristina Downing
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Department of Biochemistry, University of Oxford, Oxford, UK
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Table of contents (19 protocols)
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- Lorraine Hewitt, James M. McDonnell
Pages 1-16
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- Andrew R. Pickford, Joanne M. O’Leary
Pages 17-33
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- David Cowburn, Alexander Shekhtman, Rong Xu, Jennifer J. Ottesen, Tom W. Muir
Pages 47-56
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- Guang Zhu, Youlin Xia, Donghai Lin, Xiaolian Gao
Pages 57-78
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- Kieran Fleming, Stephen Matthews
Pages 79-88
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- Eva de Alba, Nico Tjandra
Pages 89-106
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- Christian Griesinger, Wolfgang Peti, Jens Meiler, Rafael Brüschweiler
Pages 107-122
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- Luke M. Rooney, Sachchidanand, Jörn M. Werner
Pages 123-138
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- Jennifer Blake-Hall, Olivier Walker, David Fushman
Pages 139-159
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- Guang Zhu, Youlin Xia, Donghai Lin, Xiaolian Gao
Pages 161-184
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- James G. Kempf, J. Patrick Loria
Pages 185-231
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- Daniel Nietlispach, Helen R. Mott, Katherine M. Stott, Peter R. Nielsen, Abarna Thiru, Ernest D. Laue
Pages 255-288
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- Gabriele Varani, Yu Chen, Thomas C. Leeper
Pages 289-312
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- Michael Habeck, Wolfgang Rieping, Jens P. Linge, Michael Nilges
Pages 379-402
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- Anthony Watts, Suzana K. Straus, Stephan L. Grage, Miya Kamihira, Yuen Han Lam, Xin Zhao
Pages 403-473
About this book
When I was asked to edit the second edition of Protein NMR Techniques, my first thought was that the time was ripe for a new edition. The past several years have seen a surge in the development of novel methods that are truly revolutionizing our ability to characterize biological macromolecules in terms of speed, accuracy, and size limitations. I was particularly excited at the prospect of making these techniques accessible to all NMR labs and for the opportunity to ask the experts to divulge their hints and tips and to write, practically, about the methods. I commissioned 19 chapters with wide scope for Protein NMR Techniques, and the volume has been organized with numerous themes in mind. Chapters 1 and 2 deal with recombinant protein expression using two organisms, E. coli and P. pastoris, that can produce high yields of isotopically labeled protein at a reasonable cost. Staying with the idea of isotopic labeling, Chapter 3 describes methods for perdeuteration and site-specific protonation and is the first of several chapters in the book that is relevant to studies of higher molecular weight systems. A different, but equally powerful, method that uses molecular biology to “edit” the spectrum of a large molecule using segmental labeling is presented in Chapter 4. Having successfully produced a high molecular weight target for study, the next logical step is data acquisition. Hence, the final chapter on this theme, Chapter 5, describes TROSY methods for stru- ural studies.
Reviews
From reviews of the first edition...
"...includes many good practical details which are so often omitted and which workers new to the field have to rediscover..." -Analyst
"...an excellent text... a very useful compilation...The limitations and power of the approaches are well presented and should help in experimental design very considerably." -Journal of Medicinal Chemistry
"...a collection of excellent reviews that will form a useful contribution to the bookshelf of any NMR lab." -Trends in Biotechnology
"...an excellent introduction...Readers will be left with a good understanding of the application of NMR to the study of proteins. " -Quarterly Review of Biology
Editors and Affiliations
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Department of Biochemistry, University of Oxford, Oxford, UK
A. Kristina Downing
