Probing of proteins by metal ions and their low-molecular-weight complexes
著者
書誌事項
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
大学図書館所蔵 全20件
注記
Includes bibliographical references and index
内容説明・目次
内容説明
"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."
目次
- 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.
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