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Protein NMR for the Millennium

Aus der Reihe Biological Magnetic Resonance
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144,99 € UVP 164,99 €

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Beschreibung

Produktdetails

Einband

Taschenbuch

Erscheinungsdatum

14.04.2013

Abbildungen

XII, 127 illus., 1 illus. in color., farbige Illustrationen, schwarz-weiss Illustrationen

Herausgeber

N. Rama Krishna + weitere

Verlag

Springer Us

Seitenzahl

341

Maße (L/B/H)

23,5/15,5/2 cm

Gewicht

540 g

Auflage

2002

Sprache

Englisch

ISBN

978-1-4757-8735-1

Beschreibung

Rezension

`
The book is generally easy to read for those with an appreciable knowledge of protein NMR spectroscopy. [...]presents a timely review of many recently developed techniques for the study of large proteins by NMR spectroscopy. We highly recommend it as a reference for anyone with an active interest in this field.
'

Journal of the American Chemical Society, 125:51 (2003)

Portrait

Dr. N. Rama Krishna is Professor of Biochemistry and Molecular Genetics and the Director of the NMR Core Facility at the University of Alabama at Birmingham. He has previously served as Guest Editor for Volumes 16 ( Modern Techniques in Protein NMR , 1998) and Volume 17 ( Structure Computation and Dynamics in Protein NMR , 1999). Dr. Lawrence J. Berliner is currently Professor and Chair of the Department of Chemistry and Biochemistry at the University of Denver after retiring from Ohio State University, where he spent a 32-year career in the area of biological magnetic resonance (EPR and NMR). He is the Series Editor for Biological Magnetic Resonance , which he launched in 1979.

Produktdetails

Einband

Taschenbuch

Erscheinungsdatum

14.04.2013

Abbildungen

XII, 127 illus., 1 illus. in color., farbige Illustrationen, schwarz-weiss Illustrationen

Herausgeber

Verlag

Springer Us

Seitenzahl

341

Maße (L/B/H)

23,5/15,5/2 cm

Gewicht

540 g

Auflage

2002

Sprache

Englisch

ISBN

978-1-4757-8735-1

Herstelleradresse

Springer-Verlag KG
Sachsenplatz 4-6
1201 Wien
AT

Email: GPSR Kontakt

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  • Produktbild: Protein NMR for the Millennium
  • Section I: Toward Larger Proteins in Solution and Solid State. 1. Transverse Relaxation Optimized Spectroscopy; K.V. Pervushin. 2. Segmental Isotopic Labeling: Prospects for a New Tool to Study the Structure-function Relationships in Multi-domain Proteins; J.J. Ottesen, U.K. Blaschke, D. Cowburn, T.W. Muir. 3. Characterization of Inter-Domain Orientations in Solution Using the NMR Relaxation Approach; D. Fushman, D. Cowburn. 4. Global Fold Determination of Large Proteins using Site-Directed Spin Labeling; J.L. Battiste, J.D. Gross, G. Wagner. 5. Solid State NMR Studies of Uniformly Isotopically Enriched Proteins; A. McDermott. 6. NMR Spectroscopy of Encapsulated Proteins Dissolved in Low Viscosity Fluids; A.J. Wand, C.R. Babu, P.F. Flynn, M.J. Milton. Section II: Structure Refinement. 7. Angular Restraints from Residual Dipolar Couplings for Structure Refinement; C. Griesinger, J. Meiler, W. Peti. 8. Protein Structure Refinement using Residual Dipolar Couplings; A.M. Gronenborn. 9. Hydrogen Bond Scalar Couplings - A New Tool In Biomolecular NMR; S. Grzesiek, F. Cordier, A.J. Dingley. Section III: NMR Methods for Screening Bioactive Ligands. 10. NMR Methods for Screening the Binding of Ligands to Proteins - Identification and Characterization of Bioactive Ligands; T. Peters, T. Biet, L. Herfurth. Index.