Probing of proteins by metal ions and their low-molecular-weight complexes
Author(s)
Bibliographic Information
Probing of proteins by metal ions and their low-molecular-weight complexes
（Metal ions in biological systems / edited by Helmut Sigel, v. 38）
M. Dekker, c2001
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Note
Includes bibliographical references and index
Description and Table of Contents
Description
"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.
by "Nielsen BookData"
