Protein NMR Techniques

1. Front Matter

   Pages i-xi

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2. Screening and Optimizing Protein Production in E. coli

   • Lorraine Hewitt, James M. McDonnell

   Pages 1-16

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3. Isotopic Labeling of Recombinant Proteins from the Methylotrophic Yeast Pichia pastoris

   • Andrew R. Pickford, Joanne M. O’Leary

   Pages 17-33

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4. Perdeuteration/Site-Specific Protonation Approaches for High-Molecular-Weight Proteins

   • Stephen Matthews

   Pages 35-45

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5. Segmental Isotopic Labeling for Structural Biological Applications of NMR

   • David Cowburn, Alexander Shekhtman, Rong Xu, Jennifer J. Ottesen, Tom W. Muir

   Pages 47-56

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6. TROSY-Based Correlation and NOE Spectroscopy for NMR Structural Studies of Large Proteins

   • Guang Zhu, Youlin Xia, Donghai Lin, Xiaolian Gao

   Pages 57-78

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7. Media for Studies of Partially Aligned States

   • Kieran Fleming, Stephen Matthews

   Pages 79-88

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8. Residual Dipolar Couplings in Protein Structure Determination

   • Eva de Alba, Nico Tjandra

   Pages 89-106

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9. Projection Angle Restraints for Studying Structure and Dynamics of Biomolecules

   • Christian Griesinger, Wolfgang Peti, Jens Meiler, Rafael Brüschweiler

   Pages 107-122

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10. Characterizing Domain Interfaces by NMR

    • Luke M. Rooney, Sachchidanand, Jörn M. Werner

    Pages 123-138

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11. Characterization of the Overall Rotational Diffusion of a Protein From 15N Relaxation Measurements and Hydrodynamic Calculations

    • Jennifer Blake-Hall, Olivier Walker, David Fushman

    Pages 139-159

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12. TROSY-Based NMR Experiments for the Study of Macromolecular Dynamics and Hydrogen Bonding

    • Guang Zhu, Youlin Xia, Donghai Lin, Xiaolian Gao

    Pages 161-184

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13. Measurement of Intermediate Exchange Phenomena

    • James G. Kempf, J. Patrick Loria

    Pages 185-231

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14. NMR Studies of Partially Folded Molten-Globule States

    • Christina Redfield

    Pages 233-254

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15. Structure Determination of Protein Complexes by NMR

    • Daniel Nietlispach, Helen R. Mott, Katherine M. Stott, Peter R. Nielsen, Abarna Thiru, Ernest D. Laue

    Pages 255-288

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16. NMR Studies of Protein-Nucleic Acid Interactions

    • Gabriele Varani, Yu Chen, Thomas C. Leeper

    Pages 289-312

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17. Using NMRView to Visualize and Analyze the NMR Spectra of Macromolecules

    • Bruce A. Johnson

    Pages 313-352

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18. Automated NMR Structure Calculation With CYANA

    • Peter Güntert

    Pages 353-378

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19. NOE Assignment With ARIA 2.0

    • Michael Habeck, Wolfgang Rieping, Jens P. Linge, Michael Nilges

    Pages 379-402

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20. Membrane Protein Structure Determination Using Solid-State NMR

    • Anthony Watts, Suzana K. Straus, Stephan L. Grage, Miya Kamihira, Yuen Han Lam, Xin Zhao

    Pages 403-473

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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.

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

• Department of Biochemistry, University of Oxford, Oxford, UK

  A. Kristina Downing

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