Lipid-assisted protein folding

Bogdanov, M. Dowhan, W. (1999) Lipid-assisted protein folding. J. Biol. Chem. 274, 36,827-36,830. 

Bogdanov M, Dowhan W. Lipid-assisted protein folding. / Biol Chem. 1999 274(52) 36827-36830. 

Experimental Evidence for Lipid-Assisted Folding of Proteins... 

Is lipid-assisted folding a widespread phenomenon and possibly applicable to soluble proteins The erythrocyte membrane contains about 20-mole % of PE that is almost exclusively localized in the inner leaflet and is in contact with highly concentrated heme-containing proteins. The refolding of the denatured soluble and heme-containing enzyme horseradish peroxidase (HRP) was followed in the presence and absence of liposomes made up of different phospholipids (Debnath et al., 2003). Remarkably, dimyristoyl-PE (a bilayer-forming... 

Temperature and pressure extremes require different strategies. Cellular lipids, proteins and nucleic acids are sensitive to high temperatures. Hyperthermophile bacteria have ether lipids instead of the more hydrolysis sensitive ester lipids in mesophiles [13]. Enzymes from hyperthermophiles show an unusual thermostability in the laboratory, and an important aspect of protein chemistry research is to find out the stabilizing principles. Crude cell extracts of hyperthermophiles show the presence of heat inducible proteins, called chaperones, which assist in the folding of proteins during cellular synthesis. Molecular details for cold adaptation of enzymes have been reported but are less extensively studied [14]. 

Facial amphiphilic peptides are another class of facial amphiphiles, which play an important rote in many biological processes involving lipid bilayer membranes. Because of the large surface area of the amphiphilic domains, they are prone to interact with the hydrophiUc/hydrophobic interface of lipid bilayers, which is necessary to assist in membrane fusion or transmembrane pore formation. In the case of pore-forming antibiotics, the peptides are often relatively small (between 25 and 100 amino acids) and the entire peptide becomes facially amphiphilic on folding into the secondary structure. In the case of membrane fusion or curvature-inducing proteins only the peptide fragment, which interacts with the bilayer membrane, is facially amphiphilic. 

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