EMR of Paramagnetic Molecules
Herausgegeben:Berliner, Lawrence J.; Reuben, Jacques
EMR of Paramagnetic Molecules
Herausgegeben: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.
Produktdetails
- Produktdetails
- Biological Magnetic Resonance 13
- Verlag: Springer US / Springer, Berlin
- Seitenzahl: 416
- Erscheinungstermin: 8. Mai 2013
- Englisch
- Abmessung: 229mm x 152mm x 23mm
- Gewicht: 600g
- ISBN-13: 9781461362531
- ISBN-10: 1461362539
- Artikelnr.: 39916291
- Herstellerkennzeichnung
- Libri GmbH
- Europaallee 1
- 36244 Bad Hersfeld
- gpsr@libri.de
- Biological Magnetic Resonance 13
- Verlag: Springer US / Springer, Berlin
- Seitenzahl: 416
- Erscheinungstermin: 8. Mai 2013
- Englisch
- Abmessung: 229mm x 152mm x 23mm
- Gewicht: 600g
- ISBN-13: 9781461362531
- ISBN-10: 1461362539
- Artikelnr.: 39916291
- Herstellerkennzeichnung
- Libri GmbH
- Europaallee 1
- 36244 Bad Hersfeld
- gpsr@libri.de
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.