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NMR in the Life Sciences by E. Morton Bradbury (English) Paperback Book
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Specificaties
- Objectstaat
- ISBN-13
- 9781468481808
- Book Title
- NMR in the Life Sciences
- ISBN
- 9781468481808
- Subject Area
- Science, Medical
- Publication Name
- NMR in the Life Sciences
- Publisher
- Springer
- Item Length
- 10 in
- Subject
- Spectroscopy & Spectrum Analysis, Diagnostic Imaging / General, Life Sciences / Molecular Biology, Allied Health Services / General
- Publication Year
- 2013
- Series
- NATO Science Series A: Ser.
- Type
- Textbook
- Format
- Trade Paperback
- Language
- English
- Item Height
- 0.2 in
- Item Weight
- 16.9 Oz
- Item Width
- 7 in
- Number of Pages
- VIII, 237 Pages
Over dit product
Product Identifiers
Publisher
Springer
ISBN-10
1468481800
ISBN-13
9781468481808
eBay Product ID (ePID)
175746916
Product Key Features
Number of Pages
VIII, 237 Pages
Language
English
Publication Name
NMR in the Life Sciences
Publication Year
2013
Subject
Spectroscopy & Spectrum Analysis, Diagnostic Imaging / General, Life Sciences / Molecular Biology, Allied Health Services / General
Type
Textbook
Subject Area
Science, Medical
Series
NATO Science Series A: Ser.
Format
Trade Paperback
Dimensions
Item Height
0.2 in
Item Weight
16.9 Oz
Item Length
10 in
Item Width
7 in
Additional Product Features
Intended Audience
Scholarly & Professional
Dewey Edition
19
Series Volume Number
107
Number of Volumes
1 vol.
Illustrated
Yes
Dewey Decimal
574/.028
Table Of Content
Special Problems of NMR in H2O Solution.- 2D NMR with Biopolymers.- Proton Assignment Strategies in Nucleic Acid NMR Studies.- Genetic Methods in High-REsolution NMR Studies of Proteins.- Determination of Macromolecular Structure and Dynamics by NMR.- NMR Studies of Protein-Ligand Interactions: Dihydrofolate Reductase.- Diversity of Molecular Recognition: The Combining Sites of Monoclonal Anti Spin Label Antibodies.- NMR Approaches to the Characterization of the Interaction of Metal Ions with Proteins.- Volume Selection Strategies for In Vivo Biological Spectroscopy.- The Use of Nuclear Magnetic Resonance Rotating Frame Experiments for One Dimensional Discrimination of Metabolites in Tissues.- Proton-NMR of Nuclei, Cell and Intact Tissue in Normal and Abnormal States: Significance of Relaxation Times as Correlated with Other Non-Invasive Biophysical Probes.- Towards NMR Spectroscopy In Vivo: The Use of Models.- Towards NMR Spectroscopy In Vivo: II. Relationship between NMR Parameters and Histology.- Theory of NMR Imaging.- Some Observations of NMR Imaging Particularly in Lower Fields.- Signal, Noise and R. F. Power in Magnetic Resonance Imaging.- High Field NMR Imaging and Spectroscopy.
Synopsis
This NATO Double Jump Program, held at Erice, Italy, on NMR in the Life Sciences was supported in part by contributions from Oxford Research Sys- tems, Philips International, Technicare Corporation, Varian Instruments, Sciemens Medical, and ESA Control. This program brought together three major research activities in biomedical applications of NMR: high resolu- tion NMR studies of proteins and nucleic acids, in vivo studies of animals, and NMR imaging. Whereas in the development of in vivo NMR and NMR imaging the major technological advances came initially from high resolution NMR spectroscopy, this is no longer the situation. The importance of in vivo NMR and NMR imaging in biomedical science and medical diagnosis haS-resulted in an explosion of growth in these areas involving schools of medicine, hos- pitals and instrument manufacturers. Major advances in NMR technology now come from biomedical applications of NMR as well as from high resolution NMR. Applications of high resolution NMR to the solutions structures of pro- teins and nucleic acids have been revolutionized by the development of two dimensional NMR Fourier transform techniques and the techniques of biotech- nology. Now it is possible, with small proteins up to 10,000-12,000 daltons, by 2D FT NMR techniques to follow the path of the polypeptide back- bone through the molecule. The combination of 2D FT NMR techniques with genetically engineered proteins provides one of the most powerful approaches to understanding the principles of protein folding, protein stucture and enzyme catalysis., This NATO Double Jump Program, held at Erice, Italy, on NMR in the Life Sciences was supported in part by contributions from Oxford Research Sys tems, Philips International, Technicare Corporation, Varian Instruments, Sciemens Medical, and ESA Control. This program brought together three major research activities in biomedical applications of NMR: high resolu tion NMR studies of proteins and nucleic acids, in vivo studies of animals, and NMR imaging. Whereas in the development of in vivo NMR and NMR imaging the major technological advances came initially from high resolution NMR spectroscopy, this is no longer the situation. The importance of in vivo NMR and NMR imaging in biomedical science and medical diagnosis haS-resulted in an explosion of growth in these areas involving schools of medicine, hos pitals and instrument manufacturers. Major advances in NMR technology now come from biomedical applications of NMR as well as from high resolution NMR. Applications of high resolution NMR to the solutions structures of pro teins and nucleic acids have been revolutionized by the development of two dimensional NMR Fourier transform techniques and the techniques of biotech nology. Now it is possible, with small proteins up to 10,000-12,000 daltons, by 2D FT NMR techniques to follow the path of the polypeptide back bone through the molecule. The combination of 2D FT NMR techniques with genetically engineered proteins provides one of the most powerful approaches to understanding the principles of protein folding, protein stucture and enzyme catalysis.
LC Classification Number
RA407-409.5
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