Dias, RJ, Vale TM, Lourenço JM.
2012.
Efficient Support for In-Place Metadata in Transactional Memory. Euro-Par 2012 Parallel Processing. 7484(
Kaklamanis, Christos, Papatheodorou, Theodore, Spirakis, PaulG., Eds.).:589–600., Rhodes, Greece: Springer Berlin Heidelberg
AbstractImplementations of Software Transactional Memory (STM) algorithms associate metadata with the memory locations accessed during a transaction’s lifetime. This metadata may be stored either in-place, by wrapping every memory cell in a container that includes the memory cell itself and the corresponding metadata; or out-place (also called external), by resorting to a mapping function that associates the memory cell address with an external table entry containing the corresponding metadata. The implementation techniques for these two approaches are very different and each STM framework is usually biased towards one of them, only allowing the efficient implementation of STM algorithms following that approach, hence inhibiting the fair comparison with STM algorithms falling into the other. In this paper we introduce a technique to implement in-place metadata that does not wrap memory cells, thus overcoming the bias by allowing STM algorithms to directly access the transactional metadata. The proposed technique is available as an extension to the DeuceSTM framework, and enables the efficient implementation of a wide range of STM algorithms and their fair (unbiased) comparison in a common STM infrastructure. We illustrate the benefits of our approach by analyzing its impact in two popular TM algorithms with two different transactional workloads, TL2 and multi-versioning, with bias to out-place and in-place respectively.
Gokulakrishnan, V., Parthiban, S., Elangovan, E., Jeganathan, K., Kanjilal, D., Asokan, K., Martins, Fortunato, Ramamurthi K.
2012.
Investigation of O7+ swift heavy ion irradiation on molybdenum doped indium oxide thin films. Radiation Physics and Chemistry. 81(6):589-593.
Kuckova, S, et al.
2012.
Protein identification and localization using mass spectrometry and staining tests in cross-sections of polychrome samples. Journal of Cultural Heritage.
AbstractThe identification and localization of the proteinaceous binders are essential issues in studies of painting materials and techniques, for further proposing valid restoration and conservation treatments of the painted or polychrome works of art. The challenge for analytical chemists and conservation scientists is the availability of methods able to simultaneously identify and map the presence of the binders in the multilayered structure of a sample and the possibility to use a very low amount of sample from the studied art object (considering also the criteria of minimum sampling). These methods should be fast, reproducible in different artefacts and in case of mixture of protein-based binders with other non-proteinaceous constituents (oils, resins, waxes, gums etc.) and also economical (both in terms of materials and time consume). In this context, the present paper proposes an innovative protocol of investigation using two complementary techniques – Matrix-Assisted Laser Desorption/Ionisation – Time of Flight Mass Spectrometry (MALDI-TOF MS) and staining tests (one visible and one fluorescent stain) assisted by Optical Microscopy (OM) on cross-section of samples – for the simultaneous identification and mapping of protein – and oil-based binders in paint materials. The novelty is based on the use of MALDI-TOF MS on cross-sections of paints together with a fluorescent stain for protein identification and mapping (mainly used in the area of proteomics) complementing the use of a traditional visible stain for oil-based material identification. The protocol was successfully applied on several samples taken from a Czech medieval polychrome sculpture, entitled “The Mourning of Jesus Christ” (16th century) belonging to the Moravian Gallery (Brno).
Kowacz, M, Mukhopadhyay A, Carvalho AL, Esperanca J, Romao MJ, Rebelo LPN.
2012.
Hofmeister effects of ionic liquids in protein crystallization: Direct and water-mediated interactions. Crystengcomm. 14:4912-4921., Number 15
AbstractWe have performed experiments on the crystallization of two low molecular weight, positively charged proteins, lysozyme and ribonuclease A, using ionic liquids as either crystallization additives or, in particular cases, as precipitating agents. The ionic liquids (ILs) have been ordered according to their salting-in/out ability and the relative position of these ionic liquids in this ranking has been rationalized by considering their hydration properties (positive-negative, hydrophobic-hydrophilic). The ability to screen the effective charge of cationic proteins and aid protein nucleation (salting-out) has been shown to be superior for large polarizable anions with low charge density, negatively hydrated-Cl-, Br-, [SCN](-), methane-[C1SO3](-) and ethanesulfonates [C2SO3](-), than for anions with a relatively stable hydration shell, positively hydrated-lactate [Lac](-), butylsulfonate [C4SO3](-) and acetate [Ac](-). Upon increasing the background salt concentration, where electrostatic interactions are already effectively screened, the ability of the IL ions to stabilize proteins in solution (salting-in) has been shown to increase as the ions are likely to migrate to the non-polar protein surface and lower protein-water interfacial tension. This tendency is enhanced as the focus moves from those ions with positively hydrated hydrophilic compartments (e. g. [Ac](-)) to those with negatively hydrated groups (e. g. [C1SO3](-)) and the prevailing hydrophobic hydration (e. g. [C4SO3](-)). The observed inversion in the relative effect of ILs on protein crystallization with increasing ionic strength of the aqueous media has been interpreted as the differing effects of ion adsorption: charge screening and interfacial tension modification. Moreover, this work can further help in our understanding of the influence of ionic liquids on conformational changes of biomacromolecules in solution. Identification of the specific incorporation sites for choline and acetate ions, localized in two lysozyme crystals grown in pure IL solutions without any buffer or inorganic precipitant, can give us some insight into the role of the ionic liquid ions in protein structure development.