Earthquake-triggered landslides and slope-seismic waves interaction inferring induced displacements

Earthquake-induced landslide mass mobility is a topic relevance for the analysis of earthquake induced ground effects scenarios. The landslide masses already existing on the slopes interact with the seismic waves that propagate from the bedrock, giving rise to effects of amplification of the seismic motion at specific frequencies connected to their geometry and their dynamic properties. The quantification of the earthquake-induced displacements expected in landslide masses through numerical models under dynamic conditions highlights how, especially for medium-low energy levels of the seismic input, the displacements thus obtained are generally higher than those computed by conventional approaches (e.g. Newmark method applied to the hypothesis of rigid or deformable block and related semiempirical relations). A series of case studies has also proved that the geometry of significantly dislodged landslide masses (i.e. segmented into kinematically distinct portions, namely “blocks”) due to their geomorphological evolution over time, significantly controls the seismic-induced displacements obtained by numerical models. In particular, the results highlight that the maximum displacements computed through the numerical models do not correspond to seismic inputs whose characteristic periods coincide to those of the resonance or of the length of the landslide mass but are more directly connected to the smaller dimensions of the individual blocks in which the landslide mass is segmented

Structural features of cholesterol dependent cytolysins and comparison to other MACPF-domain containing proteins.

Five different cholesterol-dependent cytolysins (CDCs) have now had their atomic structures solved. Here their structures are compared and shown to vary less in the C-terminal region than they do in their N-terminal MACPF/CDC homology region. The most variable region of the C-terminal domain is the undecapeptide, which is observed in two clusters of conformations, and comparison of this domain with the C2 domain of perforin shows that the two structures have a common ancestor. Structural studies of CDC pre-pore and pore oligomers by cryo-electron microscopy and atomic force microscopy have revealed much about their mechanism of action. Understanding the activity of CDCs has required a combination of structural, biophysical and functional assays but current models of pore formation still require development to account for variable functional pore size

Structural features of cholesterol dependent cytolysins and comparison to other MACPF-domain containing proteins.

Five different cholesterol-dependent cytolysins (CDCs) have now had their atomic structures solved. Here their structures are compared and shown to vary less in the C-terminal region than they do in their N-terminal MACPF/CDC homology region. The most variable region of the C-terminal domain is the undecapeptide, which is observed in two clusters of conformations, and comparison of this domain with the C2 domain of perforin shows that the two structures have a common ancestor. Structural studies of CDC pre-pore and pore oligomers by cryo-electron microscopy and atomic force microscopy have revealed much about their mechanism of action. Understanding the activity of CDCs has required a combination of structural, biophysical and functional assays but current models of pore formation still require development to account for variable functional pore size