Bundles of polytwins as meta-elastic domains in the thin polycrystalline simple multi-ferroic system PZT.

We used enhanced piezo-response force microscopy (E-PFM) to investigate both ferroelastic and ferroelectric nanodomains in thin films of the simple multi-ferroic system PbZr(0.3)Ti(0.7)O(3) (PZT). We show how the grains are organized into a new type of elastic domain bundles of the well-known periodic elastic twins. Here we present these bundle domains and discuss their stability and origin. Moreover, we show that they can arrange in such a way as to release strain in a more effective way than simple twinning. Finally, we show that these bundle domains can arrange to form the macroscopic ferroelectric domains that constitute the basis of ferroelectric-based memory devices.

Behavior of bulk melt-textured YBCO single domains subjected to crossed magnetic fields

We have experimentally investigated the crossed magnetic field effects on bulk melt-processed YBCO single domains. The samples were first permanently magnetized along their c-axis and then subjected to several cycles of a transverse magnetic field parallel to the ab planes. The magnetic properties along the c and ab directions were simultaneously measured using a couple of orthogonal pick-up coils as well as a Hall probe placed against the sample surface. The effects of both sweep amplitude and polarity were investigated. Field sweeps of alternate polarities are shown to affect the decay of the c-axis magnetization much more strongly than field sweeps of unique polarity do. However, the c-axis magnetization does not show any saturation even after a large number of field sweeps. Next, a micro-Hall probe scanning system was used to measure the distribution of magnetic induction over the top surface of the single domain subjected to the same combination of magnetic fields. The results are shown to be consistent with those determined with the sensing coils and bring out the role played by geometric effects.

A new protein structure of P-II class snake venom metalloproteinases: it comprises metalloproteinase and disintegrin domains

A new metalloproteinase-disintegrin, named Jerdonitin, was purified from Trimeresurus jerdonii venom with a molecular weight of 36 kDa on SDS-PAGE. It dose-dependently inhibited ADP-induced human platelet aggregation with IC50 of 120 nM. cDNA cloning and sequencing revealed that Jerdonitin belonged to the class II of snake venom metalloproteinases (SVMPs) (P-II class). Different from other P-II class SVMPs, metalloproteinase and disintegrin domains of its natural protein were not separated, confirmed by internal peptide sequencing. Compared to other P-II class SVMPs, Jerdonitin has two additional cysteines (Cys219 and Cys238) located in the spacer domain and disintegrin domain, respectively. They probably form a disulfide bond and therefore the metalloproteinase and disintegrin domains cannot be separated by posttranslationally processing. In summary, comparison of the amino acid sequences of Jerdonitin with those of other P-II class SVMPs by sequence alignment and phylogenetic analysis, in conjunction with natural protein structure data, suggested that it was a new type of P-II class SVMPs. (C) 2003 Elsevier Inc. All rights reserved.

Protein three-dimensional structural databases: Domains, structurally aligned homologues and superfamilies

This paper reports the availability of a database of protein structural domains (DDBASE), an alignment database of homologous proteins (HOMSTRAD) and a database of structurally aligned superfamilies (CAMPASS) on the World Wide Web (WWW). DDBASE contains information on the organization of structural domains and their boundaries; it includes only one representative domain from each of the homologous families. This database has been derived by identifying the presence of structural domains in proteins on the basis of inter-secondary structural distances using the program DIAL [Sowdhamini & Blundell (1995), Protein Sci. 4, 506-520]. The alignment of proteins in superfamilies has been performed on the basis of the structural features and relationships of individual residues using the program COMPARER [Sali & Blundell (1990), J. Mol. Biol. 212, 403-428]. The alignment databases contain information on the conserved structural features in homologous proteins and those belonging to superfamilies. Available data include the sequence alignments in structure-annotated formats and the provision for viewing superposed structures of proteins using a graphical interface. Such information, which is freely accessible on the WWW, should be of value to crystallographers in the comparison of newly determined protein structures with previously identified protein domains or existing families.