The dynamics of proteins in aqueous solution has been investigated through a massive approach based on ''state of the art'' molecular dynamics simulations performed for all protein metafolds using the four most popular force fields (OPLS, CHARMM, AMBER, and GROMOS). A detailed analysis of the massive database of trajectories (>1.5 terabytes of data obtained using Ϸ50 years of CPU) allowed us to obtain a robust-consensus picture of protein dynamics in aqueous solution.force field ͉ molecular dynamics ͉ molecular modeling ͉ protein structure

Summary Cancer initiating translocations such as those associated with lymphomas require the formation of paired DNA double-strand breaks (DSBs). Activation-induced cytidine deaminase (AID) produces widespread somatic mutation in mature B cells; however the extent of “off-target” DSB formation and its role in translocation-associated malignancy is unknown. Here we show that deregulated expression of AID causes widespread genome instability, which alone is insufficient to induce B cell lymphoma; transformation requires concomitant loss of the tumor suppressor p53. Mature B cell lymphomas arising as a result of deregulated AID expression are phenotypically diverse and harbor clonal reciprocal translocations involving a group of Immunoglobulin (Ig) and non-Ig genes which are direct targets of AID: this group includes miR-142, a previously unknown micro-RNA target which is translocated in human B cell malignancy. We conclude that AID produces DSBs throughout the genome, which can lead to lymphoma associated chromosome translocations in mature B cells.

NCT00692770.