G.N. la Mar (ed.)

Nuclear Magnetic Resonance of Paramagnetic Macromolecules

Herausgegeben:La Mar, G. N.

• Gebundenes Buch

Produktbeschreibung

Since A. Kowalsky's first report of the spectrum of cytochrome c in 1965, interest in the detection, assignment and interpretation of paramagnetic molecules has surged, especially in the last decade.
Two classes of systems have played a key role in the development of the field: heme proteins and iron-sulfur proteins. These two systems are unique in many respects, one of which is that they contain well-defined chromophores, each of which can be studied in detail outside the protein matrix. They are the most successfully studied macromolecules, and the first eight and last six of the seventeen contributions to this book deal with heme and/or iron-sulfur proteins. The middle three chapters survey the progress on, and significant promise of, more difficult systems which do not possess a chromophore, but which have nevertheless yielded remarkable insights into their structure.

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Produktdetails

• Nato Science Series C: 457
• Verlag: Springer / Springer Netherlands
• Artikelnr. des Verlages: 978-0-7923-3348-7
• 1995.
• Seitenzahl: 420
• Erscheinungstermin: 31. Januar 1995
• Englisch
• Abmessung: 241mm x 160mm x 28mm
• Gewicht: 762g
• ISBN-13: 9780792333487
• ISBN-10: 0792333489
• Artikelnr.: 23081122

Inhaltsangabe

New Approaches to NMR of Paramagnetic Molecules.- The Hyperfine Coupling.- Assignment Strategies and Structure Determination in Cyanide-Inhibited Heme Peroxidases.- Homology Modeling of Horseradish Peroxidase.- NMR Studies of Paramagnetic Systems to Characterise Small Molecule:Protein and Protein:Protein Interactions.- Recombinant Perdeuterated Protein as an Efficient Method for Making Unambiguous Heme Proton Resonance Assignments: Cyanide-Ligated Glycera Dibranchiata Monomer Methemoglobin Component IV as an Example.- Redox and Spin-State Control of the Activity of a Diheme Cytochrome c Peroxidase - Spectroscopic Studies.- Metalloprotein-Endor-Spectroscopy: Structure Determination of the Prosthetic Site from Randomly Oriented Specimen and Correlations with NMR-Spectroscopy.- NMR Studies of Nonheme Iron Proteins.- Cobalt Substituted Proteins.- Paramagnetic Lanthanide(III) Ions as NMR Probes for Biomolecular Structure and Function.- Chemical Functions of Single and Double NH-S Hydrogen Bond in Iron-Sulfur Metalloproteins; Model Ligands with Cys-Containing Peptide and Simple Acylaminobenzenethiolate.- 3D Structure of HiPIPs in Solution Through NMR and Molecular Dynamics Studies.- Multinuclear Magnetic Resonance and Mutagenesis Studies of Structure-Function Relationships in [2Fe-2S] Ferredoxins.- 1D and 2D Proton NMR Studies on [3Fe-4S] and [4Fe-4S] Ferredoxins Isolated from Desulfovibrio gigas.- Isotropic Proton Hyperfine Coupling in High Potential [Fe4S4]+3 Models.- Spin Dependent Electron Delocalization, Vibronic and Antiferromagnetic Couplings in Iron-Sulfur Clusters.