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Self-homodimerization of an actinoporin by disulfide bridging reveals implications for their structure and pore formation
(Nature Publishing Group, 2018-12)
The Trp111 to Cys mutant of sticholysin I, an actinoporin from Stichodactyla helianthus sea anemone, forms a homodimer via a disulfide bridge. The purified dimer is 193 times less hemolytic than the monomer. Ultracentrifugation, ...