Structure of common pili from Escherichia coli

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Abstract
Several important properties of the common pili from E. coli are discussed. These pili were resistant to the gentle Folin-Ciocalteau reagent methods for protein detection and were not readily solubilized by sodium dodecyl sulfate. They contained a reducing sugar but not peptidoglycan. The pilin had multiple conformations in sodium dodecyl sulfate [SDS] solution, and the appearance of multiple bands on SDS gels did not necessarily indicate heterogeneity of the preparation. The pilus subunit was a different protein than outer membrane protein III, which has the same apparent MW. The results of a previous study, that there is a dramatic change in the properties of pili after they are heated at pH values below 2, were confirmed.