Results 1 to 10 of about 106 (103)
On the Stability of Barrelled Topologies II [PDF]
Glasgow Mathematical Journal, 1980 If E is a Hausdorff barrelled space, which does not already have its finest locally convex topology, then the continuous dual E′ may be enlarged within the algebraic dual E*. Robertson and Yeomans [10] have recently investigated whether E can retain the barrelled property under such enlargements.
Tweddle, I., Yeomans, F. E.
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On the stability of barrelled topologies, I [PDF]
Bulletin of the Australian Mathematical Society, 1979 This note investigates, for locally convex topological vector spaces, the question of how far the property of being barrelled is stable under small increase in the size of the dual space. If the dual F of a barrelled space E is enlarged by a finite dimensional vector space M, then E remains barrelled under the new Mackey topology τ(E, F+M).
Robertson, W. J., Yeomans, F. E.
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On the stability of barrelled topologies, III [PDF]
Bulletin of the Australian Mathematical Society, 1980 Let E be a barrelled space with dual F ≠ E*. It is shown that F has uncountable codimension in E*. If M is a vector subspace of E* of countable dimension with M ∩ F = {o}, the topology τ(E, F+M) is called a countable enlargement of τ(E, F). The results of the two previous papers are extended: it is proved that a non-barrelled countable enlargement ...
Robertson, W. J. +2 more
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β-Barrel Topology of Alzheimer's β-Amyloid Ion Channels [PDF]
Journal of Molecular Biology, 2010 Emerging evidence supports the ion channel mechanism for Alzheimer's disease pathophysiology wherein small β-amyloid (Aβ) oligomers insert into the cell membrane, forming toxic ion channels and destabilizing the cellular ionic homeostasis. Solid-state NMR-based data of amyloid oligomers in solution indicate that they consist of a double-layered β ...
Jang, Hyunbum +5 more
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Cascading classifier application for topology prediction of transmembrane beta-barrel proteins [PDF]
Journal of Bioinformatics and Computational Biology, 2020 Membrane proteins are a major focus for new drug discovery. Transmembrane beta-barrel (TMB) proteins play key roles in the translocation machinery, pore formation, membrane anchoring and ion exchange. Given their key roles and the difficulty in membrane protein structure determination, the use of computational modeling is essential. This paper focuses
Hassan B. Kazemian +1 more
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BOCTOPUS: improved topology prediction of transmembrane β barrel proteins [PDF]
Bioinformatics, 2012 Abstract Motivation: Transmembrane β barrel proteins (TMBs) are found in the outer membrane of Gram-negative bacteria, chloroplast and mitochondria. They play a major role in the translocation machinery, pore formation, membrane anchoring and ion exchange. TMBs are also promising targets for antimicrobial drugs and vaccines.
Sikander Hayat, Arne Elofsson
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Denaturation of proteins with beta-barrel topology induced by guanidine hydrochloride [PDF]
Spectroscopy, 2010 The stability of the representatives of two protein classes withβ-barrel topology: porcine odorant-binding protein (OBP) and a number of fluorescent proteins (FPs), was studied. It was shown that both of them are significantly more stable than globular α-helical andα/βproteins.
Stepanenko OV +5 more
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Topological precision in the thalamic projection to neonatal mouse barrel cortex [PDF]
The Journal of Neuroscience, 1995 Somatosensory thalamus and cortex in rodents contain topological representations of the facial whisker pad. The thalamic representation of a single whisker (“barreloid”) is presumed to project exclusively to the cortical representation (“barrel”) of the same whisker; however, it was not known when this correspondence is established during early ...
Agmon, Ariel +3 more
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On barrelled topological modules [PDF]
International Journal of Mathematics and Mathematical Sciences, 1993 Some of the main theorems concerning ultrabarrelled topological vector spaces are extended to the context of topological modules.
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Examining the Flexibility of Tim Barrel Proteins Based on their Structural Topology [PDF]
Biophysical Journal, 2013 The eight-fold beta/alpha barrel-like fold, first seen in triose-phosphate isomerase (TIM), is a common and versatile fold for proteins. Proteins in this classification have diverse enzymatic functions spanning five of six Enzyme Commission classes.
Tiwari, Sandhya, Reuter, Nathalie
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