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Träfflista för sökning "WFRF:(Lagerstedt Jens O.) ;pers:(Budamagunta Madhu)"

Search: WFRF:(Lagerstedt Jens O.) > Budamagunta Madhu

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1.
  • Petrlova, Jitka, et al. (author)
  • Molecular crowding impacts the structure of apolipoprotein A-I with potential implications on in vivo metabolism and function
  • 2016
  • In: Biopolymers. - : Wiley. - 0006-3525. ; 105:10, s. 683-692
  • Journal article (peer-reviewed)abstract
    • The effect molecular crowding, defined as the volume exclusion exerted by one soluble inert molecule upon another soluble molecule, has on the structure and self-interaction of lipid-free apoA-I were explored. The influence of molecular crowding on lipid-free apoA-I oligomerization and internal dynamics has been analyzed using electron paramagnetic resonance (EPR) spectroscopy measurements of nitroxide spin label at selected positions throughout the protein sequence and at varying concentrations of the crowding agent Ficoll-70. The targeted positions include sites previously shown to be sensitive for detecting intermolecular interaction via spin–spin coupling. Circular dichroism was used to study secondary structural changes in lipid-free apoA-I imposed by increasing concentrations of the crowding agent. Crosslinking and SDS-PAGE gel analysis was employed to further characterize the role molecular crowding plays in inducing apoA-I oligomerization. It was concluded that the dynamic apoA-I structure and oligomeric state was altered in the presence of the crowding agent. It was also found that the C-terminal was slightly more sensitive to molecular crowding. Finally, the data described the region around residue 217 in the C-terminal domain of apoA-I as the most sensitive reporter of the crowding-induced self-association of apoA-I. The implications of this behavior to in vivo functionality are discussed.
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2.
  • Sengottaiyan, Palanivelu, et al. (author)
  • Characterization of the biochemical and biophysical properties of the Saccharomyces cerevisiae phosphate transporter Pho89
  • 2013
  • In: Biochemical and Biophysical Research Communications - BBRC. - : Elsevier. - 0006-291X .- 1090-2104. ; 436:3, s. 551-556
  • Journal article (peer-reviewed)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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  • Result 1-2 of 2
Type of publication
journal article (2)
Type of content
peer-reviewed (2)
Author/Editor
Lagerstedt, Jens O. (2)
Petrlova, Jitka (2)
Voss, John C. (2)
Budamagunta, Mad... (2)Undo refine
Persson, Bengt L. (1)
Domingo-Espín, Joan (1)
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Hilt, Silvia (1)
Ruiz-Pavon, Lorena (1)
Sengottaiyan, Palani ... (1)
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University
Lund University (2)
Linnaeus University (1)
Language
English (2)
Research subject (UKÄ/SCB)
Natural sciences (2)

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