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Spectroscopic Methods and Analyses NMR, Mass Spectrometry, and Metalloprotein Techniques / by Christopher Jones, Barbara Mulloy, Adrian H. Thomas.

Por: Jones, Christopher, autor.
Colaborador(es): Mulloy, Barbara, autor | Thomas, Adrian H, autor.
Series (Methods in Molecular Biology, 1940-6029; 17).Editor: Totowa, NJ : Humana Press, 1993Edición: 1st edition 1993.Descripción: 1 recurso en línea (XI, 395 páginas) : .ISBN: 9781592595044.Recursos en línea: (usuarios Universidad Europea de Valencia)Digital Resources
Contenidos:
Nmr Spectroscopy -- to Nuclear Magnetic Resonance -- Structural Studies of Proteins in Solution Using Proton Nuclear Magnetic Resonance -- Peptide Structure Determination by NMR -- High-Resolution NMR of DNA and Drug-DNA Interactions -- Structural Characterization of the Carbohydrate Moieties of Glycoproteins by High-Resolution 1H-NMR Spectroscopy -- The Application of Nuclear Magnetic Resonance to Structural Studies of Polysaccharides -- Dynamic and Exchange Processes in Macromolecules Studied by NMR Spectroscopy -- Nmr Spectroscopy -- to Mass Spectrometry -- Laser Desorption Ionization Mass Spectrometry of Bioorganic Molecules -- 252-Californium Plasma Desorption Time-of-Flight Mass Spectrometry of Peptides and Proteins -- Fast Atom Bombardment Mass Spectrometry of Peptides -- Tandem Mass Spectrometry -- Nmr Spectroscopy -- Mössbauer Spectroscopy -- Electron Paramagnetic Resonance Spectroscopy of Metalloproteins -- Resonance Raman Spectroscopy of Metalloproteins Using CW Laser Excitation -- The Application of X-Ray Absorption Spectroscopy to Characterize Metal Centers in Proteins.
Resumen: The three volumes in Methods in Molecular Biology covering Physical Methods of Analysis (vol. 1, Spectroscopic Methods and Analyses: NMR, Mass Spectrometry, and Metalloprotein Techniques; vol. 2, Optical Spectroscopy and Macroscopic Techniques; vol. 3, Cryst- lographic Methods and Techniques) differ from others in this series in several ways. Each volume covers a group of techniques for the char- terization of biological molecules and their interactions that involve the application of modern techniques of physical chemistry. These techniques by and large do not lend themselves to the "hands-on" approach and cannot usually be carried out by the molecular biologist alone, but most often require collaboration with a specialist. The biologist or biochemist contemplating such a collaboration may feel somewhat at a distance from the experimental work and further isolated by the use of the jargons of analytical and physical chemistry. Physical methods have been used in molecular biology from the earliest days, from simple applications of optical spectroscopy to the complexity of X-ray crystallography, and the full range of these me- ods will be covered over the three volumes. The methods dealt with in this first volume have largely developed from beginnings in small molecule chemistry to the point where they play a valuable role in the characterization of biological macromolecules.
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Nmr Spectroscopy -- to Nuclear Magnetic Resonance -- Structural Studies of Proteins in Solution Using Proton Nuclear Magnetic Resonance -- Peptide Structure Determination by NMR -- High-Resolution NMR of DNA and Drug-DNA Interactions -- Structural Characterization of the Carbohydrate Moieties of Glycoproteins by High-Resolution 1H-NMR Spectroscopy -- The Application of Nuclear Magnetic Resonance to Structural Studies of Polysaccharides -- Dynamic and Exchange Processes in Macromolecules Studied by NMR Spectroscopy -- Nmr Spectroscopy -- to Mass Spectrometry -- Laser Desorption Ionization Mass Spectrometry of Bioorganic Molecules -- 252-Californium Plasma Desorption Time-of-Flight Mass Spectrometry of Peptides and Proteins -- Fast Atom Bombardment Mass Spectrometry of Peptides -- Tandem Mass Spectrometry -- Nmr Spectroscopy -- Mössbauer Spectroscopy -- Electron Paramagnetic Resonance Spectroscopy of Metalloproteins -- Resonance Raman Spectroscopy of Metalloproteins Using CW Laser Excitation -- The Application of X-Ray Absorption Spectroscopy to Characterize Metal Centers in Proteins.

The three volumes in Methods in Molecular Biology covering Physical Methods of Analysis (vol. 1, Spectroscopic Methods and Analyses: NMR, Mass Spectrometry, and Metalloprotein Techniques; vol. 2, Optical Spectroscopy and Macroscopic Techniques; vol. 3, Cryst- lographic Methods and Techniques) differ from others in this series in several ways. Each volume covers a group of techniques for the char- terization of biological molecules and their interactions that involve the application of modern techniques of physical chemistry. These techniques by and large do not lend themselves to the "hands-on" approach and cannot usually be carried out by the molecular biologist alone, but most often require collaboration with a specialist. The biologist or biochemist contemplating such a collaboration may feel somewhat at a distance from the experimental work and further isolated by the use of the jargons of analytical and physical chemistry. Physical methods have been used in molecular biology from the earliest days, from simple applications of optical spectroscopy to the complexity of X-ray crystallography, and the full range of these me- ods will be covered over the three volumes. The methods dealt with in this first volume have largely developed from beginnings in small molecule chemistry to the point where they play a valuable role in the characterization of biological macromolecules.

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