AttributesValues
rdf:type
Description
  • Calmodulin is an EF hand calcium binding protein. Its binding affinities to various protein/peptide targets often depend on the conformational changes induced by the binding of calcium. One such target is melittin, which binds tightly to calmodulin in the presence of calcium, and inhibits its function. Chemical cross-linking combined with Fourier transform ion cyclotron resonance (FTICR) mass spectrometry has been employed to investigate the coordination of calmodulin and melittin in the complex at different concentrations of calcium. This methodology can be used to monitor structural changes of proteins induced by ligand binding, and study the effects these changes have on non-covalent interactions between proteins. Cross-linking results indicate that the binding place of the first melittin in the calcium free calmodulin form is the same as in the calcium loaded calmodulin/ melittin complex
  • Calmodulin is an EF hand calcium binding protein. Its binding affinities to various protein/peptide targets often depend on the conformational changes induced by the binding of calcium. One such target is melittin, which binds tightly to calmodulin in the presence of calcium, and inhibits its function. Chemical cross-linking combined with Fourier transform ion cyclotron resonance (FTICR) mass spectrometry has been employed to investigate the coordination of calmodulin and melittin in the complex at different concentrations of calcium. This methodology can be used to monitor structural changes of proteins induced by ligand binding, and study the effects these changes have on non-covalent interactions between proteins. Cross-linking results indicate that the binding place of the first melittin in the calcium free calmodulin form is the same as in the calcium loaded calmodulin/ melittin complex (en)
  • Kalmodulin je protein vážící vápník. Jeho schopnost interakce s dalšími peptidovými potažmo proteinovými partnery je závislá na jeho konformaci, která je ovlivněna přítomností vápenatých iontů. Možnost sledovat změnu konformace proteinu lze klasickými metodami, zde je presentován postup netradiční, který je založen na chemickém zesítění proteinu a následné detekci zesítěných postranních aminokyselinových zbytků pomocí hmotnostní spektrometrie vysokého rozlišení (cs)
Title
  • Monitoring conformational changes in protein complexes using chemical cross-linking and Fourier transform ion cyclotron resonance mass spectrometry: the effect of calcium binding on the calmodulin - melittin complex
  • Monitoring conformational changes in protein complexes using chemical cross-linking and Fourier transform ion cyclotron resonance mass spectrometry: the effect of calcium binding on the calmodulin - melittin complex (en)
  • Sledování změn konformace proteinového komplexu pomocí chemického zesítění a hmotnostní spektrometrie: vliv koncentrace vápníku na komplex calmodulinu a melittinu (cs)
skos:prefLabel
  • Monitoring conformational changes in protein complexes using chemical cross-linking and Fourier transform ion cyclotron resonance mass spectrometry: the effect of calcium binding on the calmodulin - melittin complex
  • Monitoring conformational changes in protein complexes using chemical cross-linking and Fourier transform ion cyclotron resonance mass spectrometry: the effect of calcium binding on the calmodulin - melittin complex (en)
  • Sledování změn konformace proteinového komplexu pomocí chemického zesítění a hmotnostní spektrometrie: vliv koncentrace vápníku na komplex calmodulinu a melittinu (cs)
skos:notation
  • RIV/61388971:_____/07:00095367!RIV08-AV0-61388971
http://linked.open.../vavai/riv/strany
  • 281;290
http://linked.open...avai/riv/aktivita
http://linked.open...avai/riv/aktivity
  • P(KJB400200501), P(LC545), Z(AV0Z50200510)
http://linked.open...iv/cisloPeriodika
  • -
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
  • 434929
http://linked.open...ai/riv/idVysledku
  • RIV/61388971:_____/07:00095367
http://linked.open...riv/jazykVysledku
http://linked.open.../riv/klicovaSlova
  • chemical cross-linking; protein confirmation; protein complex (en)
http://linked.open.../riv/klicoveSlovo
http://linked.open...odStatuVydavatele
  • GB - Spojené království Velké Británie a Severního Irska
http://linked.open...ontrolniKodProRIV
  • [2379DFA069CB]
http://linked.open...i/riv/nazevZdroje
  • European Journal of Mass Spectrometry
http://linked.open...in/vavai/riv/obor
http://linked.open...ichTvurcuVysledku
http://linked.open...cetTvurcuVysledku
http://linked.open...vavai/riv/projekt
http://linked.open...UplatneniVysledku
http://linked.open...v/svazekPeriodika
  • 13
http://linked.open...iv/tvurceVysledku
  • Novák, Petr
  • Havlíček, Vladimír
  • Bashir, S.
  • Derrick, P. J.
  • Giannakopulos, A.
  • Beran, K. A.
http://linked.open...n/vavai/riv/zamer
issn
  • 1469-0667
number of pages
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