𝔖 Bobbio Scriptorium
✦   LIBER   ✦

Metalloproteomics || Experimental Methods Used for Studies of the Binding of Metal Cations

✍ Scribed by Permyakov, Eugene A.


Book ID
126845344
Publisher
John Wiley & Sons, Inc.
Year
2009
Tongue
English
Weight
332 KB
Edition
1
Category
Article
ISBN
0470392487

No coin nor oath required. For personal study only.

✦ Synopsis


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.


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The interaction between cationic porphyrin, a potential valuable antitumor and antibiotic drug, and human serum albumin (HSA) was investigated using spectroscopy methods. The binding constants were obtained using fluorescence quenching method (K SV ΒΌ (3.24 AE 0.29) Γ‚ 10 4 M Γ€1 ) and surface plasmon