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Sökning: WFRF:(Lagerstedt Jens O.) > Tidskriftsartikel > (2010-2014)

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  • Petrlova, Jitka, et al. (författare)
  • Conformational and aggregation properties of the 1-93 fragment of apolipoprotein A-I
  • 2014
  • Ingår i: Protein Science. - : Wiley. - 1469-896X .- 0961-8368. ; 23:11, s. 71-1559
  • Tidskriftsartikel (refereegranskat)abstract
    • Several disease-linked mutations of apolipoprotein A-I, the major protein in high-density lipoprotein (HDL), are known to be amyloidogenic, and the fibrils often contain N-terminal fragments of the protein. Here, we present a combined computational and experimental study of the fibril-associated disordered 1-93 fragment of this protein, in wild-type and mutated (G26R, S36A, K40L, W50R) forms. In atomic-level Monte Carlo simulations of the free monomer, validated by circular dichroism spectroscopy, we observe changes in the position-dependent β-strand probability induced by mutations. We find that these conformational shifts match well with the effects of these mutations in thioflavin T fluorescence and transmission electron microscopy experiments. Together, our results point to molecular mechanisms that may have a key role in disease-linked aggregation of apolipoprotein A-I.
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3.
  • Sengottaiyan, Palanivelu, et al. (författare)
  • Characterization of the biochemical and biophysical properties of the Saccharomyces cerevisiae phosphate transporter Pho89
  • 2013
  • Ingår i: Biochemical and Biophysical Research Communications - BBRC. - : Elsevier. - 0006-291X .- 1090-2104. ; 436:3, s. 551-556
  • Tidskriftsartikel (refereegranskat)abstract
    • In Saccharomyces cerevisiae, Pho89 mediates a cation-dependent transport of Pi across the plasma membrane. This integral membrane protein belongs to the Inorganic Phosphate Transporter (PiT) family, a group that includes the mammalian Na+/Pi cotransporters Pit1 and Pit2. Here we report that the Pichia pastoris expressed recombinant Pho89 was purified in the presence of Foscholine-12 and functionally reconstituted into proteoliposomes with a similar substrate specificity as observed in an intact cell system. The alpha-helical content of the Pho89 protein was estimated to 44%. EPR analysis showed that purified Pho89 protein undergoes conformational change upon addition of substrate. 
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