Conformation of colicin A: Apparent difference between cytoplasmic and extracellular polypeptide chain
Martine Knibiehler, Claude J. Lazdunski
Abstract
Martine Knibiehler, Claude J. Lazdunski
Abstract
Cytoplasmic colicin A has the ability to bind to membranes and to form stable dimers. This form remains stable even in the presence of 1% SDS at 25 degrees C. Both of these properties were not observed for extracellular colicin A suggesting a possible difference in the conformation between cytoplasmic and extracellular colicin A.
OpenAlex reports 14 citations for this work. Citation counts describe recorded attention and do not establish research quality.
A contribution statement is not available in the OpenAlex record.
Method details are not available in the OpenAlex metadata.
Findings are not separately available in the OpenAlex metadata.
Limitations are not available in the OpenAlex metadata.
Application details are not available in the OpenAlex metadata.
Cytoplasmic colicin A has the ability to bind to membranes and to form stable dimers. This form remains stable even in the presence of 1% SDS at 25 degrees C. Both of these properties were not observed for extracellular colicin A suggesting a possible difference in the conformation between cytoplasmic and extracellular colicin A.
Key concepts: Colicin, Extracellular, Cytoplasm, Chemistry, Biophysics, Biochemistry, Biology, Escherichia coli