996 resultados para IMP
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Microstructures and electrochemical properties of Ti0.26Zr0.07V0.21Mn0.1Ni0.33Mox (x=0,0.025,0.05,0.075, 0.10) electrode alloys have been investigated. The results of XRD analysis show that the alloys are mainly composed of V-based solid solution phase with body centered cubic (bcc) structure and C14 Laves phase with hexagonal structure. The addition of Mo element can imp ove the activation characteristics, maximum discharge capacity and cyclic durability for the electrode alloys
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针对非线性系统传感器故障诊断难以解决的问题,提出了一种新的基于局部嵌入映射(LLE)的方法,解决了非线性数据的特征映射问题。首先,改进了基于分形维估计的内在维数的估计,通过线性拟合解决了线性区域的自动确定。然后,将故障状态与空间分布结合起来,通过确定数据点在空间超球内的分布完成故障的检测,在这个过程中将超球的确定与LLE算法中基于核函数的样本外数据扩展结合起来,大大减少了计算量,提高了算法的实时性,从而为复杂非线性传感器的故障诊断提供了一种新的有效的方法。
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Signaturas: [ ]1, [*]4, [¶]-2[¶]4, 3[¶]8, A-Z4, 2A-2L4 ; [ ]2, A-Z4, 2A-2K4 ; [ ]2, A-Z4, 2A-2Q4.
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Signaturas: *6, A-F4, G2, H-Z4, 2A-2Z4, 3A-3Z4, 4A-4Z4, 5A-5D4, 5E2, 5F4 ; *5, A-Z4, 2A-2Z4, 3A-3Y4, Z2, 4A4 ; *5, A-Z4, 2A-2Z4, 3A-3Z4, 4A-4N4, 4O5 ; *5, A-Z4, 2A-2Z4, 3A-3Z4, 4A-4O4, 4P2, 4Q1, 4R4 ; *5, A-Z4, 2A-2Z4, 3A-3M4, *2, A-S4.
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En Tomo V. 2 h. de grabados calcográficos representando monedas de Huesca.
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Editio novissima cui praeter Annotationes Emanuelis Suarez a Ribeira, accesserunt Illustrationes, sive Additiones Joannis de Ayllon Laynez in fine cujusque Capitis appositae, cum Indice Generali.
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Error tipográfico en el pie de imprenta del t. I: --Castilpa-ren-- en lugar de --Castilla-ren--
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Signaturas: [¶]4, A-Q8, R4.
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Colofón en v.1, v.2, v.5, v.6, y v.7.
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Nunc primum simul edita, ad codices mss. recognita, nonnullis notis illustrata atque in duos tomos distributa.
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Nueva impresion, en la qual van puestas las adiciones del Suplemento en sus lugares.
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Signaturas: a-d4, A-Z4, 2A-2Z4, 3A-3H4.
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Quarta impresion.
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The BUZ/Znf-UBP domain is a protein module found in the cytoplasmic deacetylase HDAC6, E3 ubiquitin ligase BRAP2/IMP, and a subfamily of ubiquitin-specific proteases. Although several BUZ domains have been shown to bind ubiquitin with high affinity by recognizing its C-terminal sequence (RLRGG-COOH), it is currently unknown whether the interaction is sequence-specific or whether the BUZ domains are capable of binding to proteins other than ubiquitin. In this work, the BUZ domains of HDAC6 and Ubp-M were subjected to screening against a one-bead-one-compound (OBOC) peptide library that exhibited random peptide sequences with free C-termini. Sequence analysis of the selected binding peptides as well as alanine scanning studies revealed that the BUZ domains require a C-terminal Gly-Gly motif for binding. At the more N-terminal positions, the two BUZ domains have distinct sequence specificities, allowing them to bind to different peptides and/or proteins. A database search of the human proteome on the basis of the BUZ domain specificities identified 11 and 24 potential partner proteins for Ubp-M and HDAC6 BUZ domains, respectively. Peptides corresponding to the C-terminal sequences of four of the predicted binding partners (FBXO11, histone H4, PTOV1, and FAT10) were synthesized and tested for binding to the BUZ domains by fluorescence polarization. All four peptides bound to the HDAC6 BUZ domain with low micromolar K(D) values and less tightly to the Ubp-M BUZ domain. Finally, in vitro pull-down assays showed that the Ubp-M BUZ domain was capable of binding to the histone H3-histone H4 tetramer protein complex. Our results suggest that BUZ domains are sequence-specific protein-binding modules, with each BUZ domain potentially binding to a different subset of proteins.