Metal Ions in Biological Systems
Volume 38: Probing of Proteins by Metal Ions and Their Low-Molecular-Weight Complexes
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"Focuses on the vibrant area of probing enzymes or proteins by metal ions and small complexes. Offers a summary of the basic characteristics of the amide bond, emphasizing its proton and metal ion interactions, including a quantitative analysis of its hydrolysis and formation."
Table of Contents
Peptide bond characteristics; lanthanide ion-mediated peptide hydrolysis; the cobalt(III)-promoted hydrolysis of amides and small peptides; synthetic copper(II) and nickel(II) peptidases; palladium(II) and platinum(II) complexes as synthetic peptides; protease activity of 1,10-phenanthroline-copper systems; specific protein degradation of copper(II) ions; artificial ion-dependent proteases; hydroxyl-radical footprinting of proteins using metal ion complexes; nickel- and cobalt-dependent oxidation and cross-linking of proteins; effects of metal ions on the oxidation and nitrozation of cysteine residues in proteins and enzymes; protein cross-linking mediated by metal ion complexes; ferrocenoyl amino acids and peptides - probing peptide structure; synthetic analogues of zinc enzymes; mimicking biological electron transfer and oxygen activation involving ion and copper proteins - a bio(in)organic supramolecular approach.
". . .continues the long and excellent tradition established by the Metal Ions in the Biological Systems series. . .a must for all chemistry, biology, and medical libraries. "
Journal of the American Chemical Society