配有冷却风扇的永磁电机三维热分析

Overheating of permanent magnet (PM) machines has become a major technical challenge as it gives rise to magnet demagnetization, degradation of insulation materials, and loss of motor efficiency. This paper proposes a state-of-the-art cooling system for an axial flux permanent magnet (AFPM) machine with the focus on its structural optimization. A computational fluid dynamics (CFD) simulation with thermal consideration has been shown to be an efficient approach in the literature and is thus employed in this work. Meanwhile, a simplified numerical approach to the AFPM machine with complex configuration in 3D consisting of conduction, forced convection, and conjugate heat transfer is taken as a case study. Different simplification methods (including configuration and working conditions) and two optimized fans for forced convection cooling are designed and installed on the AFPM machine and compared to a natural convection cooling system. The results show that the proposed approach is effective for analyzing the thermal performance of a complex AFPM machine and strikes a balance between reasonable simplification, accuracy, and computational resource

A Subset of Chaperones and Folding Enzymes Form Multiprotein Complexes in Endoplasmic Reticulum to Bind Nascent Proteins

We demonstrate the existence of a large endoplasmic reticulum (ER)-localized multiprotein complex that is comprised of the molecular chaperones BiP; GRP94; CaBP1; protein disulfide isomerase (PDI); ERdj3, a recently identified ER Hsp40 cochaperone; cyclophilin B; ERp72; GRP170; UDP-glucosyltransferase; and SDF2-L1. This complex is associated with unassembled, incompletely folded immunoglobulin heavy chains. Except for ERdj3, and to a lesser extent PDI, this complex also forms in the absence of nascent protein synthesis and is found in a variety of cell types. Cross-linking studies reveal that the majority of these chaperones are included in the complex. Our data suggest that this subset of ER chaperones forms an ER network that can bind to unfolded protein substrates instead of existing as free pools that assembled onto substrate proteins. It is noticeable that most of the components of the calnexin/calreticulin system, which include some of the most abundant chaperones inside the ER, are either not detected in this complex or only very poorly represented. This study demonstrates an organization of ER chaperones and folding enzymes that has not been previously appreciated and suggests a spatial separation of the two chaperone systems that may account for the temporal interactions observed in other studies