Annealing response of the intermetallic alloy Ti-22Al-25Nb

A hot rolled two-phase Ti-22Al-25Nb (at.%) alloy containing the orthorhombic (O) and beta(B2) phases was subjected to thermal treatment under different conditions. The experiment was aimed to examine the recrystallization response of the beta(B2) phase (static and dynamic) to microstructure and crystallographic texture evolution using scanning electron microscopy coupled with electron backscattered diffraction (SEM-EBSD). Specimens rolled in the two-phase (O + beta(B2)) region consisted of highly deformed beta(B2) grains. The texture was close to that of the typical bcc deformation texture with a few additional texture components. A subsequent heat treatment of these rolled specimens in single beta(B2) phase region was characterized by static recrystallized beta(B2) grains with the final texture partly inherited from as-rolled material. In contrast, specimens rolled in the single beta(B2) region produced beta(B2) grains with the texture similar to that of completely dynamic recrystallized one. (C) 2010 Elsevier Ltd. All rights reserved.

Enantiospecific total synthesis of ent-5-senceioyloxy-10,11-epoxythapsan-10-ol

Enantiospecific total synthesis of optical antipode of the sesquiterpene 5-senecioyloxy-10,11-epoxythapsan-10-ol has been described. (R)-Carvone has been employed as the chiral starting material and a combination of intramolecular alkyation and Criegee fragmentation are employed for intramolecular stereospecific transfer of the chirality. An intramolecular diazoketone cyclopropanation and regioselective cyclopropane ring cleavage reactions have been employed or the creation of the three requisite contiguous quaternary carbon atoms.

HARMONY: a server for the assessment of protein structures

Protein structure validation is an important step in computational modeling and structure determination. Stereochemical assessment of protein structures examine internal parameters such as bond lengths and Ramachandran (phi, psi) angles. Gross structure prediction methods such as inverse folding procedure and structure determination especially at low resolution can sometimes give rise to models that are incorrect due to assignment of misfolds or mistracing of electron density maps. Such errors are not reflected as strain in internal parameters. HARMONY is a procedure that examines the compatibility between the sequence and the structure of a protein by assigning scores to individual residues and their amino acid exchange patterns after considering their local environments. Local environments are described by the backbone conformation, solvent accessibility and hydrogen bonding patterns. We are now providing HARMONY through a web server such that users can submit their protein structure files and, if required, the alignment of homologous sequences. Scores are mapped on the structure for subsequent examination that is useful to also recognize regions of possible local errors in protein structures. HARMONY server is located at http://caps.ncbs.res.in/harmony/