About: Study of chaperone-like activity of human haptoglobin: conformational changes under heat shock conditions and localization of interaction sites.     Goto   Sponge   NotDistinct   Permalink

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  • With respect to the mechanism of chaperone-like activity, we examined the behaviour of haptoglobin under heat shock conditions. Secondary structure changes during heat treatment were followed by circular dichroism, Raman spectroscopy and infrared spectroscopy. A model of the haptoglobin tetramer, based on its sequence homology with serine proteases and the CCP modules, has been proposed. Sequence regions responsible for the chaperone-like activity were not fully identical with the region that took part in formation of the hemoglobin-haptoglobin complex. We can postulate presence of at least two different chaperone-binding sites on each haptoglobin heavy chain.
  • With respect to the mechanism of chaperone-like activity, we examined the behaviour of haptoglobin under heat shock conditions. Secondary structure changes during heat treatment were followed by circular dichroism, Raman spectroscopy and infrared spectroscopy. A model of the haptoglobin tetramer, based on its sequence homology with serine proteases and the CCP modules, has been proposed. Sequence regions responsible for the chaperone-like activity were not fully identical with the region that took part in formation of the hemoglobin-haptoglobin complex. We can postulate presence of at least two different chaperone-binding sites on each haptoglobin heavy chain. (en)
Title
  • Study of chaperone-like activity of human haptoglobin: conformational changes under heat shock conditions and localization of interaction sites.
  • Study of chaperone-like activity of human haptoglobin: conformational changes under heat shock conditions and localization of interaction sites. (en)
skos:prefLabel
  • Study of chaperone-like activity of human haptoglobin: conformational changes under heat shock conditions and localization of interaction sites.
  • Study of chaperone-like activity of human haptoglobin: conformational changes under heat shock conditions and localization of interaction sites. (en)
skos:notation
  • RIV/67985823:_____/02:20030020!RIV/2004/AV0/A20004/N
http://linked.open.../vavai/riv/strany
  • 1667;1676
http://linked.open...avai/riv/aktivita
http://linked.open...avai/riv/aktivity
  • Z(AV0Z5011922), Z(MSM 113100001)
http://linked.open...iv/cisloPeriodika
  • 10
http://linked.open...vai/riv/dodaniDat
http://linked.open...aciTvurceVysledku
http://linked.open.../riv/druhVysledku
http://linked.open...iv/duvernostUdaju
http://linked.open...titaPredkladatele
http://linked.open...dnocenehoVysledku
  • 665699
http://linked.open...ai/riv/idVysledku
  • RIV/67985823:_____/02:20030020
http://linked.open...riv/jazykVysledku
http://linked.open.../riv/klicovaSlova
  • chaperone; haptoglobin; molecular modeling (en)
http://linked.open.../riv/klicoveSlovo
http://linked.open...odStatuVydavatele
  • DE - Spolková republika Německo
http://linked.open...ontrolniKodProRIV
  • [839934B23E81]
http://linked.open...i/riv/nazevZdroje
  • Biological Chemistry
http://linked.open...in/vavai/riv/obor
http://linked.open...ichTvurcuVysledku
http://linked.open...cetTvurcuVysledku
http://linked.open...ocetUcastnikuAkce
http://linked.open...nichUcastnikuAkce
http://linked.open...UplatneniVysledku
http://linked.open...v/svazekPeriodika
  • 383
http://linked.open...iv/tvurceVysledku
  • Hofbauerová, Kateřina
  • Baumruk, V.
  • Kopecký jr., V.
  • Ettrich, R.
  • Pavlíček, Z.
  • Brandt, W.
http://linked.open...n/vavai/riv/zamer
issn
  • 1431-6730
number of pages
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