Protein NMR Spectroscopy

Informationen zum Autor Dr. Cavanagh is the William Neal Reynolds Distinguished Professor of Biochemistry at North Carolina State University. He is an expert in protein structural biology, particularly in how bacteria are able to protect themselves. Dr. Cavanagh received his Ph.D. in Chemistry/NMR spectroscopy from the University of Cambridge in 1988. He has held positions as a Senior Research Associate at The Scripps Research Institute, Director of Structural Biology at the Wadsworth Center (New York State Department of Health), Associate Professor of Biomedical Sciences (SUNY) and Professor of Chemistry (Purdue). Since 2000 he has been Professor of Biochemistry in the Department of Molecular & Structural Biochemistry at North Carolina State University. Dr. Cavanagh has served on numerous NIH and NSF grant review panels and is currently a permanent member of the MSFB Study Section at NIH . He has authored over 100 peer-reviewed research publications and has been awarded the Foulerton Gift & Binmore Kenner Fellowship of the Royal Society (1990), the Fullsome Award (1996), the NC State University Alumni Associations Outstanding Research Award (2005) and Entrepreneur of the Year- NC State University (2012). He runs the Jimmy V-NCSU Cancer Therapeutics Training Program, was Assistant Vice Chancellor for Research at NC State from 2012-2014 and is the co-founder and Chief Scientific Officer of Agile Sciences Inc., a Raleigh based biotechnology company focusing on antibiotic resistance. Klappentext The field of NMR spectroscopy has changed a good deal since the first edition of this extremely successful book was published in 1996. The authors have extensively updated the book, it now includes an additional chapter explaining new models of spin relaxation theory and conformation changes. Combines a theoretical treatment of NMR spectroscopy with an exposition of the experimental techniques applicable to proteins. This work describes measurement and use of residual dipolar coupling constants for structure determination, TROSY and deuterium labeling for application to large macromolecules. It also includes NMR spectra of ubiquitin....

Autorentext
Dr. Cavanagh is the William Neal Reynolds Distinguished Professor of Biochemistry at North Carolina State University. He is an expert in protein structural biology, particularly in how bacteria are able to protect themselves. Dr. Cavanagh received his Ph.D. in Chemistry/NMR spectroscopy from the University of Cambridge in 1988. He has held positions as a Senior Research Associate at The Scripps Research Institute, Director of Structural Biology at the Wadsworth Center (New York State Department of Health), Associate Professor of Biomedical Sciences (SUNY) and Professor of Chemistry (Purdue). Since 2000 he has been Professor of Biochemistry in the Department of Molecular & Structural Biochemistry at North Carolina State University. Dr. Cavanagh has served on numerous NIH and NSF grant review panels and is currently a permanent member of the MSFB Study Section at NIH . He has authored over 100 peer-reviewed research publications and has been awarded the Foulerton Gift & Binmore Kenner Fellowship of the Royal Society (1990), the Fullsome Award (1996), the NC State University Alumni Associations Outstanding Research Award (2005) and Entrepreneur of the Year- NC State University (2012). He runs the Jimmy V-NCSU Cancer Therapeutics Training Program, was Assistant Vice Chancellor for Research at NC State from 2012-2014 and is the co-founder and Chief Scientific Officer of Agile Sciences Inc., a Raleigh based biotechnology company focusing on antibiotic resistance.

Klappentext

The field of NMR spectroscopy has changed a good deal since the first edition of this extremely successful book was published in 1996. The authors have extensively updated the book, it now includes an additional chapter explaining new models of spin relaxation theory and conformation changes.

Zusammenfassung
Combines a theoretical treatment of NMR spectroscopy with an exposition of the experimental techniques applicable to proteins. This work describes measurement and use of residual dipolar coupling constants for structure determination, TROSY and deuterium labeling for application to large macromolecules. It also includes NMR spectra of ubiquitin.

Inhalt
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