Attention to orientation, size, luminance, and color: Attentional failure within the form domain.

1994 ◽  
Vol 20 (1) ◽  
pp. 61-80 ◽  
Author(s):  
Muriel Boucart ◽  
Glyn W. Humphreys
Keyword(s):  
Form Domain

A laser diffraction and nuclear magnetic resonance investigation of the cholesteric potassium N-dodecanoylalaninate mesophase system

1985 ◽  
Vol 63 (1) ◽  
pp. 95-99 ◽  
Author(s):  
Keith Radley ◽  
Alan S. Tracey
Keyword(s):  
Optical Purity ◽  
Major Axis ◽  
Laser Diffraction ◽  
Diamagnetic Anisotropy ◽  
Twisted Nematic ◽  
Nuclear Magnetic Resonance Investigation ◽  
Magnetic Resonance Investigation ◽  
The Individual ◽  
Form Domain ◽  
The Magnetic Field

Nematic and twisted nematic mesophases have been prepared from various mixtures of potassium N-dodecanoyl-l-alaninate and its racemate. The induced pitch was determined as a function of optical purity as were nmr spectra from a variety of additives including several inorganic salts and d,l-alanine. Dipolar couplings from the CHCH3 moiety of the alaninate headgroup were studied, as were quadrupole splittings from the N—D of the amido group and the D2O of the water. It was proposed that with development of cholesteric behaviour on proceeding in a stepwise fashion from the d,l to l amphiphile, the individual disk-like micelles twisted into a chiral shape, then aggregated to form domain-like structures. The major axis of these aggregates is the axis along which the helix propagates and this local axis serves as the director axis for the aggregates. The individual aggregates reorient as a unit when placed in the magnetic field of an nmr spectrometer. As a consequence of this, the diamagnetic anisotropy of the mesophase prepared from the l amphiphile is positive in sign while that of the d,l analogue is negative. Despite this observed change in diamagnetic anisotropy, the alignment of the individual micelles is not different for the chiral and racemic materials.

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

1997 ◽  
Vol 12 (9) ◽  
pp. 2366-2373 ◽  
Author(s):  
K. Parlinski ◽  
Y. Kawazoe
Keyword(s):  
Monoclinic Phase ◽  
Domain Walls ◽  
Symmetry Axis ◽  
Antiphase Domain ◽  
Annealing Process ◽  
Domain Pattern ◽  
Lead Phosphate ◽  
Calculated Density ◽  
Domain Structures ◽  
Form Domain

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.

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

Mathematics ◽  
2022 ◽  
Vol 10 (2) ◽  
pp. 218
Author(s):  
Aitor Balmaseda ◽  
Davide Lonigro ◽  
Juan Manuel Pérez-Pardo
Keyword(s):  
Schrödinger Equation ◽  
Schrodinger Equation ◽  
Functional Expression ◽  
Linear Operators ◽  
Time Dependent ◽  
Bounded Linear ◽  
Sesquilinear Forms ◽  
Constant Form ◽  
Form Domain ◽  
Differentiability Properties

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.

Domain structures in rapidly solidified Mn76Fe4Si20 alloys

1990 ◽  
Vol 48 (4) ◽  
pp. 1010-1011
Author(s):  
D. S. Zhou ◽  
W. Cao ◽  
Z.X. Jin ◽  
H.Q. Ye
Keyword(s):  
Electron Diffraction ◽  
Diffraction Pattern ◽  
Domain Structure ◽  
Electron Diffraction Pattern ◽  
Unit Cell ◽  
Domain Structures ◽  
Planar Fault ◽  
Rapidly Solidified ◽  
Form Domain ◽  
Similar Domain

In the study course of microstructures of the rapidly quenched Mn-Si alloy, 45° rotation twins showing striking eightfold symmetry in the electron diffraction pattern have been reported. These previous investigations interpreted the domain structures in terms of the β-Mn phase. The aim of this work is to show the similar domain structure having pseudo-eightfold symmetry in the reciprocal space in the Mn-Fe-Si system and to ascertain a new structure in the domain structure.The main phase in this alloy is the β-Mn phase with primitive cubic and a=0.63 nm. Fig.l gives the [001] HR image of the β-Mn phase where a square unit cell has been outlined. A planar fault showing projected rectangle network was also seen.The short edge of the rectangle remains to be the same as the a axis of the p-Mn phase, while its long side is equal to . The planar fault could appear repeatedly and form domain structure as shown in Fig.2.

The HPr Proteins from the Thermophile Bacillus stearothermophilus can form Domain-swapped Dimers

2005 ◽  
Vol 346 (3) ◽  
pp. 919-931 ◽  
Author(s):  
Sudharsan Sridharan ◽  
Abbas Razvi ◽  
J. Martin Scholtz ◽  
James C. Sacchettini
Keyword(s):  
Bacillus Stearothermophilus ◽  
Form Domain

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

2015 ◽  
Author(s):  
Olga V Stepanenko ◽  
Denis O Roginskii ◽  
Olesya V Stepanenko ◽  
Irina M Kuznetsova ◽  
Vladimir N Uversky ◽  
...  
Keyword(s):  
Ligand Binding ◽  
Disulfide Bond ◽  
Binding Proteins ◽  
Odorant Binding Protein ◽  
Double Mutation ◽  
Odorant Binding Proteins ◽  
Glycine Residue ◽  
Natural Ligand ◽  
Odorant Binding ◽  
Form Domain

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.

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

2015 ◽  
Author(s):  
Olga V Stepanenko ◽  
Denis O Roginskii ◽  
Olesya V Stepanenko ◽  
Irina M Kuznetsova ◽  
Vladimir N Uversky ◽  
...  
Keyword(s):  
Ligand Binding ◽  
Disulfide Bond ◽  
Binding Proteins ◽  
Odorant Binding Protein ◽  
Double Mutation ◽  
Odorant Binding Proteins ◽  
Glycine Residue ◽  
Natural Ligand ◽  
Odorant Binding ◽  
Form Domain

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.

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

2019 ◽  
Author(s):  
Yitao Cai ◽  
Xiaojun Wan
Keyword(s):  
Classification Performance ◽  
Attention Mechanism ◽  
Sentiment Classification ◽  
Classification Model ◽  
Word Embeddings ◽  
Classification Models ◽  
Domain Specific ◽  
Proposed Model ◽  
Public Datasets ◽  
Form Domain

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.

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

PeerJ ◽  
2016 ◽  
Vol 4 ◽  
pp. e1574 ◽  
Author(s):  
Olga V. Stepanenko ◽  
Denis O. Roginskii ◽  
Olesya V. Stepanenko ◽  
Irina M. Kuznetsova ◽  
Vladimir N. Uversky ◽  
...  
Keyword(s):  
Ligand Binding ◽  
Disulfide Bond ◽  
Binding Proteins ◽  
Odorant Binding Protein ◽  
Double Mutation ◽  
Odorant Binding Proteins ◽  
Glycine Residue ◽  
Natural Ligand ◽  
Odorant Binding ◽  
Form Domain

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.

Sign in / Sign up

Export Citation Format

Share Document