On the Schrödinger Equation for Time-Dependent Hamiltonians with a Constant Form Domain

We study two seminal approaches, developed by B. Simon and J. Kisyński, to the well-posedness of the Schrödinger equation with a time-dependent Hamiltonian. In both cases, the Hamiltonian is assumed to be semibounded from below and to have a constant form domain, but a possibly non-constant operator domain. The problem is addressed in the abstract setting, without assuming any specific functional expression for the Hamiltonian. The connection between the two approaches is the relation between sesquilinear forms and the bounded linear operators representing them. We provide a characterisation of the continuity and differentiability properties of form-valued and operator-valued functions, which enables an extensive comparison between the two approaches and their technical assumptions.

Multi-Domain Sentiment Classification Based on Domain-Aware Embedding and Attention

Sentiment classification is a fundamental task in NLP. However, as revealed by many researches, sentiment classification models are highly domain-dependent. It is worth investigating to leverage data from different domains to improve the classification performance in each domain. In this work, we propose a novel completely-shared multi-domain neural sentiment classification model to learn domain-aware word embeddings and make use of domain-aware attention mechanism. Our model first utilizes BiLSTM for domain classification and extracts domain-specific features for words, which are then combined with general word embeddings to form domain-aware word embeddings. Domain-aware word embeddings are fed into another BiLSTM to extract sentence features. The domain-aware attention mechanism is used for selecting significant features, by using the domain-aware sentence representation as the query vector. Evaluation results on public datasets with 16 different domains demonstrate the efficacy of our proposed model. Further experiments show the generalization ability and the transferability of our model.

Structure and stability of recombinant bovine odorant-binding protein: II. Unfolding of the monomeric forms

In a family of monomeric odorant-binding proteins (OBPs), bovine OBP (bOBP), that lacks conserved disulfide bond found in other OBPs, occupies unique niche because of its ability to form domain-swapped dimers. In this study, we analyzed conformational stabilities of the recombinant bOBP and its monomeric variants, the bOBP-Gly121+ mutant containing an additional glycine residue after the residue 121 of the bOBP, and the GCC-bOBP mutant obtained from the bOBP-Gly121+ form by introduction of the Trp64Cys/His155Cys double mutation to restore the canonical disulfide bond. We also analyzed the effect of the natural ligand binding on the conformational stabilities of these bOBP variants. Our data are consistent with the conclusion that the unfolding-refolding pathways of the recombinant bOBP and its mutant monomeric forms bOBP-Gly121+ and GCC-bOBP are similar and do not depend on the oligomeric status of the protein. This clearly shows that the information on the unfolding-refolding mechanism is encoded in the structure of the bOBP monomers. However, the process of the bOBP unfolding is significantly complicated by the formation of the domain-swapped dimer, and the rates of the unfolding-refolding reactions essentially depend on the conditions in which the protein is located.

Structure and stability of recombinant bovine odorant-binding protein: II. Unfolding of the monomeric forms

In a family of monomeric odorant-binding proteins (OBPs), bovine OBP (bOBP), that lacks conserved disulfide bond found in other OBPs, occupies unique niche because of its ability to form domain-swapped dimers. In this study, we analyzed conformational stabilities of the recombinant bOBP and its monomeric variants, the bOBP-Gly121+ mutant containing an additional glycine residue after the residue 121 of the bOBP, and the GCC-bOBP mutant obtained from the bOBP-Gly121+ form by introduction of the Trp64Cys/His155Cys double mutation to restore the canonical disulfide bond. We also analyzed the effect of the natural ligand binding on the conformational stabilities of these bOBP variants. Our data are consistent with the conclusion that the unfolding-refolding pathways of the recombinant bOBP and its mutant monomeric forms bOBP-Gly121+ and GCC-bOBP are similar and do not depend on the oligomeric status of the protein. This clearly shows that the information on the unfolding-refolding mechanism is encoded in the structure of the bOBP monomers. However, the process of the bOBP unfolding is significantly complicated by the formation of the domain-swapped dimer, and the rates of the unfolding-refolding reactions essentially depend on the conditions in which the protein is located.

Structure and stability of recombinant bovine odorant-binding protein: II. Unfolding of the monomeric forms

In a family of monomeric odorant-binding proteins (OBPs), bovine OBP (bOBP), that lacks conserved disulfide bond found in other OBPs, occupies unique niche because of its ability to form domain-swapped dimers. In this study, we analyzed conformational stabilities of the recombinant bOBP and its monomeric variants, the bOBP-Gly121+ mutant containing an additional glycine residue after the residue 121 of the bOBP, and the GCC-bOBP mutant obtained from the bOBP-Gly121+ form by introduction of the Trp64Cys/His155Cys double mutation to restore the canonical disulfide bond. We also analyzed the effect of the natural ligand binding on the conformational stabilities of these bOBP variants. Our data are consistent with the conclusion that the unfolding-refolding pathways of the recombinant bOBP and its mutant monomeric forms bOBP-Gly121+ and GCC-bOBP are similar and do not depend on the oligomeric status of the protein. This clearly shows that the information on the unfolding-refolding mechanism is encoded in the structure of the bOBP monomers. However, the process of the bOBP unfolding is significantly complicated by the formation of the domain-swapped dimer, and the rates of the unfolding-refolding reactions essentially depend on the conditions in which the protein is located.

Domain pattern formation in ferroelastic Pb3(PO4)2 by computer simulation

A model of lead phosphate, which describes the rhombohedral-monoclinic phase transition, is used to form domain patterns in the annealing process. The obtained domain structures show W and W′ types of domain walls in agreement with the stress-free laws proposed in Sapriel's theory. The observed W domain walls are parallel to the ternary symmetry axis, while the W′ ones are tilted with respect to the same axis. The antiphase domain walls take no preferential orientations, and remain parallel to the ternary axis. The calculated density of the potential energy of the domain wall of type W is estimated to be Edw = 49 K/Å2 at T = 300 K.