scispace - formally typeset
Journal ArticleDOI

Coordinating properties of the amide bond. Stability and structure of metal ion complexes of peptides and related ligands

Helmut Sigel, +1 more
- 01 Aug 1982 - 
- Vol. 82, Iss: 4, pp 385-426
Reads0
Chats0
About
This article is published in Chemical Reviews.The article was published on 1982-08-01. It has received 1459 citations till now. The article focuses on the topics: Metal–ligand multiple bond & Peptide bond.

read more

Citations
More filters
Journal ArticleDOI

The Hofmeister effect and the behaviour of water at interfaces.

TL;DR: The first general, detailed qualitative molecular mechanism for the origins of ion-specific (Hofmeister) effects on the surface potential difference at an air-water interface is proposed; this mechanism suggests a simple model for the behaviour of water at all interfaces, regardless of whether the non-aqueous component is neutral or charged, polar or non-polar.
Journal ArticleDOI

Ions from the Hofmeister series and osmolytes: effects on proteins in solution and in the crystallization process.

TL;DR: The surface potential difference and surface tension at an air-salt solution interface are used to generate a simple model for how ions affect protein stability and solubility through indirect interactions at the protein-solution interface.
Journal ArticleDOI

Formation Mechanism of Carbogenic Nanoparticles with Dual Photoluminescence Emission

TL;DR: This work presents a systematic investigation of the formation mechanism of carbogenic nanoparticles (CNPs), otherwise referred to as C-dots, by following the pyrolysis of citric acid (CA)-ethanolamine (EA) precursor at different temperatures.
Journal ArticleDOI

Characterization of copper interactions with alzheimer amyloid beta peptides: identification of an attomolar-affinity copper binding site on amyloid beta1-42.

TL;DR: A ligand displacement technique that uses metal-chelator complexes to evaluate metal ion binding to Abeta, a notoriously self-aggregating peptide, indicated that there is a very-high-affinity Cu(2+)-binding site on Abeta1-42 that mediates peptide precipitation and that the tendency of this peptide toSelf-aggregate in aqueous solutions is due to the presence of trace metal contamination.
Related Papers (5)