3 research outputs found
Integrated motor drives: state of the art and future trends
With increased need for high power density, high efficiency and high temperature capabilities in Aerospace and Automotive applications, Integrated Motor Drives (IMD) offers a potential solution. However, close physical integration of the converter and the machine may also lead to an increase in components temperature. This requires careful mechanical, structural and thermal analysis; and design of the IMD system.
This paper reviews existing IMD technologies and their thermal effects on the IMD system. The effects of the power electronics (PE) position on the IMD system and its respective thermal management concepts are also investigated. The challenges faced in designing and manufacturing of an IMD along with the mechanical and structural impacts of close physical integration is also discussed and potential solutions are provided. Potential converter topologies for an IMD like the Matrix converter, 2-level Bridge, 3-level NPC and Multiphase full bridge converters are also reviewed. Wide band gap devices like SiC and GaN and their packaging in power modules for IMDs are also discussed. Power modules components and packaging technologies are also presented
The human transketolase-like proteins TKTL1 and TKTL2 are bona fide transketolases
CITATION: Deshpande, G. P., Patterton, H. G. & Essop, M. F. 2019. The human transketolase-like proteins TKTL1 and TKTL2 are bona fide transketolases. BMC Structural Biology, 19:2, doi:10.1186/s12900-018-0099-y.Background: Three transketolase genes have been identified in the human genome to date: transketolase (TKT),
transketolase-like 1 (TKTL1) and transketolase-like 2 (TKTL2). Altered TKT functionality is strongly implicated in the
development of diabetes and various cancers, thus offering possible therapeutic utility. It will be of great value to
know whether TKTL1 and TKTL2 are, similarly, potential therapeutic targets. However, it remains unclear whether
TKTL1 and TKTL2 are functional transketolases.
Results: Homology modelling of TKTL1 and TKTL2 using TKT as template, revealed that both TKTL1 and TKTL2
could assume a folded structure like TKT. TKTL1/2 presented a cleft of suitable dimensions between the homodimer
surfaces that could accommodate the co-factor-substrate. An appropriate cavity and a hydrophobic nodule were
also present in TKTL1/2, into which the diphosphate group fitted, and that was implicated in aminopyrimidine and
thiazole ring binding in TKT, respectively. The presence of several identical residues at structurally equivalent
positions in TKTL1/2 and TKT identified a network of interactions between the protein and co-factor-substrate,
suggesting the functional fidelity of TKTL1/2 as transketolases.
Conclusions: Our data support the hypothesis that TKTL1 and TKTL2 are functional transketolases and represent
novel therapeutic targets for diabetes and cancer.https://bmcstructbiol.biomedcentral.com/articles/10.1186/s12900-018-0099-yPublisher's versio