|
|
|
|
| LEADER |
04852nmm a2200301 u 4500 |
| 001 |
EB000714390 |
| 003 |
EBX01000000000000000567472 |
| 005 |
00000000000000.0 |
| 007 |
cr||||||||||||||||||||| |
| 008 |
140122 ||| eng |
| 020 |
|
|
|a 9789400995246
|
| 100 |
1 |
|
|a Bertini, I.
|e [editor]
|
| 245 |
0 |
0 |
|a ESR and NMR of Paramagnetic Species in Biological and Related Systems
|h Elektronische Ressource
|b Proceedings of the NATO Advanced Study Institute held at Acquafredda di Maratea, Italy, June 3–15,1979
|c edited by I. Bertini, R. Drago
|
| 250 |
|
|
|a 1st ed. 1980
|
| 260 |
|
|
|a Dordrecht
|b Springer Netherlands
|c 1980, 1980
|
| 300 |
|
|
|a XX, 434 p
|b online resource
|
| 505 |
0 |
|
|a 6. Intermediate Spin; S = 3/2 -- 7. Non-Haem Iron Sulphur Clusters -- XI: ESR and NMR Spectra of Exchange Coupled Metal Ions -- 1. The Nature of the Exchange Interaction -- 2. Effect of Exchange on the Magnetic Resonance Spectra -- XII: Iron Sulfur Proteins: Combined Mössbauer and EPR Studies -- 1. Introduction -- 2. Some Basic Features of 57Fe Mössbauer Spectroscopy -- 3. Paramagnetic Hyperfine Structure and Connection with EPR Data -- 4. Mossbauer and EPR Studies of Nitrogenase -- XIII: The Spin-Pairing Model for the Binding of Dioxygen to Transition Metal Complexes -- 1. Introduction -- 2. The Spin-Pairing Model -- 3. Electron Transfer Analysis -- 4. The Isotropic Cobalt Hyperfine Coupling Constant -- 5. Relevance of the Spin-Pairing Model to Hemoglobin Cooperativity -- XIV: EPR Studies of Copper Centers in Proteins -- 1. Introduction -- 2. Copper-Proteins Containing all the Copper in a Form that is not Detected by EPR in the Native States --
|
| 505 |
0 |
|
|a 8. Discussion -- V: Multiple Pulse 1H NMR Experiments for Structural Studies of Hemoproteins -- 1. Introduction -- 2. Multiple Pulse Experiments -- 3. Recent Applications of Multiple Pulse Experiments for Structural Studies of Hemoproteins -- VI: Nuclear Magnetic Resonance Studies of Paramagnetic Proteins -- 1. Introduction -- 2. Paramagnetic Shifts -- 3. Hemes -- VII : Paramagnetic Ions as Relaxation Probes in Biological Systems -- 1. Introduction -- 2. Theory -- 3. Applications -- 4. Conclusions -- VIII: Theory of Electron Spin Resonance -- 1. S = 1/2 Systems -- 2. S = 3/2 and 5/2 Systems -- 3. Pseudo S = 1/2 Systems -- IX: The Electronic Ground State of 3d Metal Ions with Respect to the ESR and NMR Experiment -- 1. Survey of General Theory -- 2. The ESR Experiment -- 3. The NMR Experiment -- X: EPR of Iron in Biological Systems -- 1. Introduction -- 2. High-Spin Ferrous; S =2 -- 3. Low-Spin Ferric; S = 1/2 -- 4. High-Spin Ferric; S = 5/2 -- 5. Spin Equilibria; S = 5/2, 1/2 --
|
| 505 |
0 |
|
|a I: Pulse Techniques and Nuclear Spin Relaxation -- 1. Spin-Lattice and Spin-Spin Relaxation Mechanisms -- 2. Experimental Techniques for the Measurement of T1, T2, Tp, and the NOE -- 3. Two-Dimensional (2D) NMR Spectroscopy -- II: Architecture and Dynamics of Isotopically Labelled Macromolecules by Nuclear Magnetic Resonance Spectroscopy -- 1. Introduction -- 2. Red Blood Cell Suspensions -- 3. Structural Constituents of Cells -- 4. 13c Labelled Enzymes: Dihydrofolate Reductase -- 5. Concluding Remarks -- III: Contact and Dipolar NMR Shifts: Theory and Applications -- 1. Introduction -- 2. Contact Shifts -- 3. Dipolar Shifts -- IV: Solvent Nuclear Magnetic Relaxation Dispersion (NMRD) in Solutions of Paramagnetic Proteins. A Critical Analysis, by Example -- 1. Introduction -- 2. Concanavalin A Data -- 3. Traditional SBM Theory -- 4. Comparison of Data with Traditional SBM Theory -- 5. Another Approach to SBM -- 6. Implications of the New View -- 7. Critique of the Parameters --
|
| 505 |
0 |
|
|a 3. Copper-Proteins where all the Copper Exists as an EPR-Detectable Form: the Mononuclear Cu( II) -Proteins -- 4. Copper-Proteins with Partially EPR-Detectable Copper: the Proteins with Multiple Copper Centers that Reduce 02 to H20 -- XV: The Binding of Divalent Ions to Transfer Nucleic Acids -- 1. Introduction -- 2. EPR Titration of Manganese Binding to tRNA -- 3. EPR of Bound Manganese -- 4. Phosphorus NMR and Relaxation of tRNA -- 5. A Polyelectrolyte Theory of Binding of Manganese to tRNA -- XVI: Physical Studies of Azurin and Some Metal Replaced Derivatives -- 1. Introduction -- 2. Spectral Studies of Azurin and its Metal Replaced Derivatives -- 3. Summary -- XVII: Physical Aspects of the Spin Labelling Technique -- 1.Nitroxide Radicals can give Information about Motion -- 2. Conventional EPR: 10-10
|
| 653 |
|
|
|a Chemistry
|
| 700 |
1 |
|
|a Drago, R.
|e [editor]
|
| 041 |
0 |
7 |
|a eng
|2 ISO 639-2
|
| 989 |
|
|
|b SBA
|a Springer Book Archives -2004
|
| 490 |
0 |
|
|a Nato Science Series C:, Mathematical and Physical Sciences
|
| 028 |
5 |
0 |
|a 10.1007/978-94-009-9524-6
|
| 856 |
4 |
0 |
|u https://doi.org/10.1007/978-94-009-9524-6?nosfx=y
|x Verlag
|3 Volltext
|
| 082 |
0 |
|
|a 540
|