Probing of proteins by metal ions and their low-molecular-weight complexes / edited by Astrid Sigel and Helmut Sigel.
Saved in:
Online Access: |
Full Text (via Taylor & Francis) |
---|---|
Other Authors: | , |
Format: | eBook |
Language: | English |
Published: |
[New York, N.Y.] :
Marcel Dekker, Inc.,
2001.
|
Series: | Metal ions in biological systems ;
v. 38. |
Subjects: |
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.