Structure and biogenesis of the capsular F1 antigen from Yersinia pestis: Preserved folding energy drives fiber formation

Most gram-negative pathogens express fibrous adhesive virulence organelles that mediate targeting to the sites of infection. The F1 capsular antigen from the plague pathogen Yersinia pestis consists of linear fibers of a single subunit (Caf1) and serves as a prototype for nonpilus organelles assembled via the chaperone/usher pathway. Genetic data together with high-resolution X-ray structures corresponding to snapshots of the assembly process reveal the structural basis of fiber formation. Comparison of chaperone bound Caf1 subunit with the subunit in the fiber reveals a novel type of conformational change involving the entire hydrophobic core of the protein. The observed conformational change suggests that the chaperone traps a high-energy folding intermediate of Caf1. A model is proposed in which release of the subunit allows folding to be completed, driving fiber formation.

Radiometric analysis of the light coupled by optimally cut plastic optical fiber amplitude modulating reflectance displacement sensors

A radiometric analysis of the light coupled by optical fiber amplitude modulating extrinsic-type reflectance displacement sensors is presented. Uncut fiber sensors show the largest range but a smaller responsivity. Single cut fiber sensors exhibit an improvement in responsivity at the expense of range. A further increase in responsivity as well as a reduction in the operational range is obtained when the double cut sensor configuration is implemented. The double cut configuration is particularly suitable in applications where feedback action is applied to the moving reflector surface. © 2000 American Institute of Physics.