1987•FEBS LettersRequires access

Conformation of colicin A: Apparent difference between cytoplasmic and extracellular polypeptide chain

Martine Knibiehler, Claude J. Lazdunski

Open publisher page 14 citations

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.

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What this paper is about

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.

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Available 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.

Key concepts: Colicin, Extracellular, Cytoplasm, Chemistry, Biophysics, Biochemistry, Biology, Escherichia coli

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