| Literature DB >> 9241423 |
Abstract
Zinc-finger domains are small metal-binding modules that are found in a wide range of gene regulatory proteins. Peptides corresponding to these domains have provided valuable model systems for examining a number of biophysical parameters entirely unrelated to their nucleic acid binding properties. These include the chemical basis for metal-ion affinity and selectivity, thermodynamic properties related to hydrophobic packing and beta-sheet propensities, and constraints on the generation of ligand-binding and potential catalytic sites. These studies have laid the foundation for applications such as the generation of optically detected zinc probes and the design of metal-binding peptides and proteins with desired spectroscopic and chemical properties.Entities:
Mesh:
Substances:
Year: 1997 PMID: 9241423 DOI: 10.1146/annurev.biophys.26.1.357
Source DB: PubMed Journal: Annu Rev Biophys Biomol Struct ISSN: 1056-8700