α-Synuclein in central nervous system and from erythrocytes, mammalian cells, and Escherichia coli exists predominantly as disordered monomer
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Aerolysin is one of a large group of bacterial proteins that can kill target cells by forming discrete channels in their plasma membranes. The toxin has many properties in common with the porins of the Gram-negative bacterial outer membrane, including an e ...
The pore-forming alpha-toxin from Staphylococcus aureus is secreted as a soluble monomeric protein. In order to form a transmembrane channel, the protein has to undergo oligomerization and membrane insertion. Previous studies have shown that channel format ...
Membrane proteins fulfill many central functions in the biological membrane. The insertion process of these proteins and their structure, which are intimately linked to their function, are not yet well understood. As a model we studied three proteins recon ...
The 'molten' globular conformation of a protein is compact with a native secondary structure but a poorly defined tertiary structure. Molten globular states are intermediates in protein folding and unfolding and they may be involved in the translocation or ...
The secondary structure of bacterio-opsin (BO), the retinal free protein-component of bacteriorhodopsin (BR), was detd. by Raman spectroscopy. Addnl. CD measurements revealed only negligible conformational differences between BO in apomembranes and BR in p ...
Aerolysin is a channel-forming protein secreted as a protoxin by Aeromonas hydrophila. Analytical centrifugation measurements showed that proaerolysin is a dimer in solution, and this was confirmed by chemical cross-linking with dimethyl suberimidate. Diss ...
The secondary structure of lactose permease (I) of Escherichia coli reconstituted in lipid membranes was detd. by Raman spectroscopy. The a-helix content was .apprx.70%, the b-strand content was
The secondary structure of porin, maltoporin, and OmpA protein reconstituted in lipid membranes was detd. by Raman spectroscopy. The 3 proteins have similar structures consisting of 50-60% b-strand, .apprx.20% b-turn, and
Different molecular masses have been assigned to the human interferon-gamma receptor (HuIFN-gamma-R) by several authors. After extensive purification from Raji cells, this receptor was shown in a previous work to consist of two major protein species with m ...
