Simulation of Continuous Dynamic Recrystallization Using a Level-Set Method.

Dynamic recrystallization is one of the main phenomena responsible for microstructure evolution during hot forming. Consequently, obtaining a better understanding of dynamic recrystallization mechanisms and being able to predict them is crucial. This paper proposes a full-field numerical framework to predict the evolution of subgrain structures upon grain growth, continuous dynamic recrystallization, and post-dynamic recrystallization.

Folded structures in protonated reduced dipeptides.

Reduced dipeptides with the general formula RCO-Xaa-rXbb-N+HR'R" (rXbb, reduced analogue of residue Xbb: NH-C alpha HR1-CrH2) are shown to adopt a folded conformation in solution and in the solid state. The protonated reduced amide bond is an active proton donor capable of interacting with a peptide carbonyl to give a strong hydrogen bond topologically equivalent to the i+2 or i+3-->i interaction. The resulting conformation is similar to the y- or beta-turn structure found in peptides and proteins.

Structure of tBuCO-Gly-Gly psi [CH2-N+H2]NHEt.BPh4-.

N-(tert-Butylcarbonylglycylaminoethyl)-N-(ethyl)ammonium tetraphenylborate, C11H24N3O+2.C24H20B-, Mr = 549.57, triclinic, P-1, a = 11.