EMR of Paramagnetic Molecules (eBook, PDF)
Redaktion: Berliner, Lawrence J.; Reuben, Jacques
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EMR of Paramagnetic Molecules (eBook, PDF)
Redaktion: Berliner, Lawrence J.; Reuben, Jacques
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Published as a companion to Volume 12, the current volume presents the latest advances in electron paramagnetic resonance of iron proteins, metalloproteins, and free radicals. The book features a diskette containing programs for iron ERP spectral simulation and ENDOR analyses.
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Published as a companion to Volume 12, the current volume presents the latest advances in electron paramagnetic resonance of iron proteins, metalloproteins, and free radicals. The book features a diskette containing programs for iron ERP spectral simulation and ENDOR analyses.
Dieser Download kann aus rechtlichen Gründen nur mit Rechnungsadresse in A, B, BG, CY, CZ, D, DK, EW, E, FIN, F, GR, HR, H, IRL, I, LT, L, LR, M, NL, PL, P, R, S, SLO, SK ausgeliefert werden.
Produktdetails
- Produktdetails
- Verlag: Springer US
- Seitenzahl: 400
- Erscheinungstermin: 6. Dezember 2012
- Englisch
- ISBN-13: 9781461528920
- Artikelnr.: 44179017
- Verlag: Springer US
- Seitenzahl: 400
- Erscheinungstermin: 6. Dezember 2012
- Englisch
- ISBN-13: 9781461528920
- Artikelnr.: 44179017
- Herstellerkennzeichnung Die Herstellerinformationen sind derzeit nicht verfügbar.
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.
1 Simulation of the EMR Spectra of High-Spin Iron in Proteins.- 1. Introduction.- 2. Theoretical Background for Simulations.- 3. Examples of Simulated Lineshapes.- References.- 2 Mössbauer Spectroscopy of Iron Proteins.- 1. Introduction.- 2. Mössbauer Effect: Spectral Parameters.- 3. Iron-Sulfur Proteins.- 4. Heme Proteins.- 5. Mononuclear Iron Proteins.- 6. Oxygen-Bridged Dinuclear Clusters.- References.- 3 Multifrequency ESR of Copper: Biophysical Applications.- 1. Introduction.- 2. The Role of Microwave Frequency for Different Rotational Correlation Times.- 3. Multifrequency Apparatus and Methods.- 4. Biophysical Applications of Multifrequency ESR.- 5. Perspectives.- References.- 4 Metalloenzyme Active-Site Structure and Function through Multifrequency CW and Pulsed ENDOR.- 1. Introduction.- 2. The ENDOR Measurement.- 3. Multiple Approaches in ENDOR.- 4. ENDOR as the Solution to Problems about Metallobiomolecules.- 5. Metalloenzymes with Amino Acid Radicals.- 6. Conclusion.- Appendix: ENDOR Analysis...- References.- 5 ENDOR of Randomly Oriented Mononuclear Metalloproteins: Toward Structural Determinations of the Prosthetic Group.- 1. Introduction.- 2. Theory.- 3. Examples.- 4. Conclusion.- References.- 6 High-Field EPR and ENDOR on Bioorganic Systems.- 1. Introduction.- 2. Basic Principles and Overview.- 3. High-Field EPR/ENDOR in Photosynthesis Research.- 4. Perspectives.- References.- 7 Pulsed Electron Nuclear Double and Multiple Resonance Spectroscopy of Metals in Proteins and Enzymes.- 1. Introduction.- 2. ENDOR Energy Levels and Transition Frequencies.- 3. Pulse Schemes.- 4. Amplitudes in Polarization Transfer Pulsed ENDOR.- 5. Pulsed versus CW ENDOR.- 6. ESEEM versus ENDOR Spectroscopy.- 7. Electron Nuclear Electron Triple Resonance: 2D ENDOR.- 8. ConcludingRemarks.- References.- 8 Transient EPR of Spin-Labeled Proteins.- 1. Introduction.- 2. Methods.- 3. Time-Resolved EPR of Contractile Proteins.- 4. Time-Resolved EPR of Membrane Proteins.- 5. Conclusions.- References.- 9 ESR Spin-Trapping Artifacts in Biological Model Systems.- 1. Introduction.- 2. Nitroso Spin Traps.- 3. Nitrone Spin Traps.- 4. Conclusion.- References.- of Previous Volumes.
1 Simulation of the EMR Spectra of High-Spin Iron in Proteins.- 1. Introduction.- 2. Theoretical Background for Simulations.- 3. Examples of Simulated Lineshapes.- References.- 2 Mössbauer Spectroscopy of Iron Proteins.- 1. Introduction.- 2. Mössbauer Effect: Spectral Parameters.- 3. Iron-Sulfur Proteins.- 4. Heme Proteins.- 5. Mononuclear Iron Proteins.- 6. Oxygen-Bridged Dinuclear Clusters.- References.- 3 Multifrequency ESR of Copper: Biophysical Applications.- 1. Introduction.- 2. The Role of Microwave Frequency for Different Rotational Correlation Times.- 3. Multifrequency Apparatus and Methods.- 4. Biophysical Applications of Multifrequency ESR.- 5. Perspectives.- References.- 4 Metalloenzyme Active-Site Structure and Function through Multifrequency CW and Pulsed ENDOR.- 1. Introduction.- 2. The ENDOR Measurement.- 3. Multiple Approaches in ENDOR.- 4. ENDOR as the Solution to Problems about Metallobiomolecules.- 5. Metalloenzymes with Amino Acid Radicals.- 6. Conclusion.- Appendix: ENDOR Analysis...- References.- 5 ENDOR of Randomly Oriented Mononuclear Metalloproteins: Toward Structural Determinations of the Prosthetic Group.- 1. Introduction.- 2. Theory.- 3. Examples.- 4. Conclusion.- References.- 6 High-Field EPR and ENDOR on Bioorganic Systems.- 1. Introduction.- 2. Basic Principles and Overview.- 3. High-Field EPR/ENDOR in Photosynthesis Research.- 4. Perspectives.- References.- 7 Pulsed Electron Nuclear Double and Multiple Resonance Spectroscopy of Metals in Proteins and Enzymes.- 1. Introduction.- 2. ENDOR Energy Levels and Transition Frequencies.- 3. Pulse Schemes.- 4. Amplitudes in Polarization Transfer Pulsed ENDOR.- 5. Pulsed versus CW ENDOR.- 6. ESEEM versus ENDOR Spectroscopy.- 7. Electron Nuclear Electron Triple Resonance: 2D ENDOR.- 8. ConcludingRemarks.- References.- 8 Transient EPR of Spin-Labeled Proteins.- 1. Introduction.- 2. Methods.- 3. Time-Resolved EPR of Contractile Proteins.- 4. Time-Resolved EPR of Membrane Proteins.- 5. Conclusions.- References.- 9 ESR Spin-Trapping Artifacts in Biological Model Systems.- 1. Introduction.- 2. Nitroso Spin Traps.- 3. Nitrone Spin Traps.- 4. Conclusion.- References.- of Previous Volumes.