Synthesizes the current knowledge in the field and provides new insights into medical applications
Metalloproteomics is the large-scale study of metal-binding proteins. These proteins, which represent about one quarter of all the proteins in the Protein Data Bank, play important roles in all biological systems and all biological processes. Metalloproteomics provides the latest information on all major families of metal-binding proteins, including their structural, physico-chemical, and functional properties, enabling readers to better understand these proteins. Moreover, the book demonstrates how understanding the structures, properties, and functions of intracellular and extracellular metal-binding proteins may unlock the key to drug development for the treatment of a myriad of diseases.
Written by Eugene Permyakov, an international expert and pioneer in the structural analysis of metal-binding proteins, the book offers
- Theoretical introduction to cation binding
- Broad range of methods for investigating the binding of different cations to proteins
- Characteristics of interactions of physiologically important cations of Ca, Mg, Zn, Fe, Mn, Co, Cu, Ni, Mo, W, Na, and K with proteins
- Detailed considerations of structural and physico-chemical properties of the metal-binding proteins
- Interactions of all other metal cations with proteins
- Interactions of different types of cations with nucleic acids
Throughout the text, the author integrates principles of proteomics. In addition, detailed examples underscore the role metal-binding proteins play in health and medicine.
Bringing together and analyzing all the latest findings, Metalloproteomics' scope and level of insight are unparalleled. It is recommended for biophysicists, biochemists, enzymologists, cell and molecular biologists, protein and peptide scientists, organic and bioinorganic chemists, and chemical biologists.
Table of Contents
1. The complexes of metal cations with low molecular mass compounds and proteins.
- 1.1. Biologically significant metal cations.
- 1.2. Structures and properties of the complexes of metal cations with low molecular mass compounds.
- 1.3. Dissociation constants for complexes of metal cations with low molecular mass compounds.
- 1.4. Solubilities of complexes of calcium and some other metal cations.
2. General regularities of the binding of metal cations to proteins.
- 2.1. The structures of the protein binding sites of calcium, magnesium, zinc and transition metal ions.
- 2.2. Binding stoichiometry and binding (dissociation) constants.
- 2.3. Protein families.
3. Experimental methods used for studies of the binding of metal cations.
- 3.1. Atomic flame absorption spectroscopy.
- 3.2. Radioactivity.
- 3.3. Ion selective electrodes.
- 3.4. Calcium buffers.
- 3.5. Equilibrium and flow dialysis.
- 3.6. Fluorescent dyes.
- 3.7. Isothermal titration calorimetry.
- 3.8. Differential scanning calorimetry.
- 3.9. Absorption spectroscopy.
- 3.10. Fluorescent spectroscopy.
- 3.11. Circular dichroism and optical rotatory dispersion spectroscopy.
- 3.13. Extended X-ray absorption fine structure spectroscopy.
- 3.14. Small angle X-ray scattering.
- 3.15. Proteolysis.
- 3.16. Deuterium exchange.
- 3.17. Crystallography.
- 3.18. Nuclear magnetic resonance.
- 3.19. Electron spin resonance.
- 3.20. Mussbauer spectroscopy.
4. Calcium, calcium binding proteins and their major families.
- 4.1. EF-hand proteins.
- 4.2. Other Cytosolic Proteins That May Be Calcium Modulated.
- 4.3. Extracellular calcium binding proteins.
5. Interactions of calcium binding proteins with low molecular mass compounds, peptides, proteins and membranes.
- 5.1. Interactions with low molecular mass compounds.
- 5.2. Interactions with peptides and proteins.
- 5.3. Interactions with membrane systems.
6. Calcium binding proteins in various systems.
- 6.1. Calcium binding proteins in muscles.
- 6.2. Calcium binding proteins in nervous system.
- 6.3. Participation of calcium binding proteins in blood coagulation process.
- 6.4. Participation of calcium binding proteins in the calcification of hard tissues.
- 6.5. Cytotoxic activity of calcium binding proteins.
- 6.6. Calcium binding proteins in bacteria.
7. The binding of magnesium ions to proteins.
8. The binding of zinc ions to proteins.
- 8.1. Structural zinc binding sites.
- 8.2. Catalytic zinc binding sites.
- 8.3. Co-catalytic zinc binding sites.
- 8.4. Protein interface zinc binding sites.
- 8.5. The binding of zinc ions to calcium binding proteins.
- 8.6. Some general notes on zinc binding sites.
- 8.7. Zinc ions in cells.
9. The binding of copper ions to proteins.
- 9.1. Multicopper blue proteins.
- 9.2. Monocopper blue proteins.
- 9.3. Binuclear CuA sites.
- 9.4. Copper transport and anti-copper protection.
- 9.5. Interactions of copper with prion proteins.
- 9.6. Alzheimer?s and Parkinson?s diseases and metal cations.
- 9.7. Wilson and Menkes disease and copper ions.
10. Iron binding proteins.
- 10.1. Iron-containing heme-proteins.
- 10.2. Transferrin and lactoferrin.
- 10.3. Ferritin and bacterioferritin.
- 10.4. The proteins with Fe-S clasters.
- 10.5. Bacterial iron homeostasis.
11. Molybdenum- and tungsten-containing proteins.
- 11.1. Xanthine oxidase.
- 11.2. Sulfite oxidase.
- 11.3. MSO-reductase.
- 11.4. ldehyde:ferredoxin oxidoreductase and formaldehyde:ferredoxin oxidoreductase.
12. Proteins containing nickel and cobalt.
- 12.1. Urease.
- 12.2. Methionine aminopeptidase.
- 12.3. Nitrile hydratase.
13. Manganese-containing proteins.
- 13.1. Manganese in the photosynthetic systems.
- 13.2. Manganese-containing enzymes.
14. Sodium- and potassium-binding proteins.
- 14.1. Potassium channel.
- 14.2. Sodium pump.
- 14.3. The mammalian Na+/H+ exchanger.
- 14.4. Na+/Ca2+ exchanger.
- 14.5. Enzymes activated by monovalent cations.
15. Interactions of metal cations with nucleic acids.
- 15.1. Interactions of metal cations with DNA.
- 15.2. Interactions of metal cations with RNA.
16. "Non-physiological" metals.
- 16.1. Alkali metals.
- 16.2. Alkali-earth metals.
- 16.3. Transition metals.
- 16.4. Metals and metalloids in the Groups 13-16.
17. Concluding remarks.
EUGENE PERMYAKOV, PhD, Doctor of Sciences, Professor of Biophysics, has been the Director of the Institute for Biological Instrumentation of the Russian Academy of Sciences since 1994. His research focuses on the study of physico-chemical and functional properties of metal-binding proteins, with an emphasis on calcium-binding proteins.