Dynamic and structural properties of sphinogolipids as driving forces for the formation of membrane domains

Article Abstract:

Sphingolipids, components of the membranes of all living organism cells, are abundant in the plasma membranes and show a strong amphiphilic character, being constituted by a two-tail hydrophobic moiety, ceramide and a very structurally variable hydrophilic headgroup. The peculiar physicochemical properties of sphingolipids and experimental data suggest that they play an active role in the biogenesis and maintenance of membrane lipid domains, where proteins involved in processes of cell signaling are segregated and can exert their properties.

Oligosaccharides, Structure, Chemical properties, Hydrophobic effect, Membrane lipids

---

Structural and functional aspects of metal sites in biology

Article Abstract:

The classification of metal sites in biomolecules on the basis of structural and functional analysis gives five basic types of classes. These are structural configuration of the protein, storage of metals, electron transfer, dioxygen binding for metal-O2 coordination and catalytic activity. Crystallography establishes the geometric structure of these biomolecules. The metalloprotein sites enable the proteins to act as ligands.

Usage, Observations, Crystallography, Molecular structure, Metalloproteins

---

Similar abstracts:

• Abstracts: Structural, spectroscopic, and reactivity models for the manganese catalyses
• Abstracts: Structural and chemical properties of silyl radicals. Silicon-tethered reactions. Direct kinetic studies of silicon hydride radicals in the gas phase
• Abstracts: Structural and chemical properties of silyl radicals. Silsesquioxanes
• Abstracts: Chemistry, design, and structure-activity relationship of cocaine antagonists. Structure and chemistry of cytochrome P450
• Abstracts: Antifreeze proteins: structures and mechanisms of function. Synthetic models for heme-copper oxidases. Electronic structures of metal sites in proteins and models: contributions to function in blue copper proteins

This website is not affiliated with document authors or copyright owners. This page is provided for informational purposes only. Unintentional errors are possible.