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  • Using the title methods, the denaturation of human hemoglobin and its subunits was studied, the ultimate goal being to assess the applicability of both methods in research on pathogenic protein mutations. Pulse proteolysis affords a denaturation curve of hemoglobin; the mehod is easy to perform showing good repeatability and low sample consumption. Using the limited proteolysis followed by MALDI-TOF MS, we studied proteolytic resistance of fragments of a- and b-globin chains. Despite their nearly identical structure, the differences in amino acid compositions of both polypeptides affect the conformational stability of their tryptic products. Both methods are able to provide valuable information on protein stability, their main advantage being low cost and simplicity.
  • Using the title methods, the denaturation of human hemoglobin and its subunits was studied, the ultimate goal being to assess the applicability of both methods in research on pathogenic protein mutations. Pulse proteolysis affords a denaturation curve of hemoglobin; the mehod is easy to perform showing good repeatability and low sample consumption. Using the limited proteolysis followed by MALDI-TOF MS, we studied proteolytic resistance of fragments of a- and b-globin chains. Despite their nearly identical structure, the differences in amino acid compositions of both polypeptides affect the conformational stability of their tryptic products. Both methods are able to provide valuable information on protein stability, their main advantage being low cost and simplicity. (en)
  • Using the title methods, the denaturation of human hemoglobin and its subunits was studied, the ultimate goal being to assess the applicability of both methods in research on pathogenic protein mutations. Pulse proteolysis affords a denaturation curve of hemoglobin; the mehod is easy to perform showing good repeatability and low sample consumption. Using the limited proteolysis followed by MALDI-TOF MS, we studied proteolytic resistance of fragments of a- and b-globin chains. Despite their nearly identical structure, the differences in amino acid compositions of both polypeptides affect the conformational stability of their tryptic products. Both methods are able to provide valuable information on protein stability, their main advantage being low cost and simplicity. (cs)
Title
  • Limitovaná a pulzní proteolýza lidského hemoglobinu
  • Limited and Pulse Proteolysis of Human Hemoglobin (en)
  • Limitovaná a pulzní proteolýza lidského hemoglobinu (cs)
skos:prefLabel
  • Limitovaná a pulzní proteolýza lidského hemoglobinu
  • Limited and Pulse Proteolysis of Human Hemoglobin (en)
  • Limitovaná a pulzní proteolýza lidského hemoglobinu (cs)
skos:notation
  • RIV/60461373:22330/10:00024238!RIV11-MSM-22330___
http://linked.open...avai/riv/aktivita
http://linked.open...avai/riv/aktivity
  • Z(MSM6046137305)
http://linked.open...iv/cisloPeriodika
  • 4
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
  • 268531
http://linked.open...ai/riv/idVysledku
  • RIV/60461373:22330/10:00024238
http://linked.open...riv/jazykVysledku
http://linked.open.../riv/klicovaSlova
  • Hemoglobin; Pulse proteolysis; Limited proteolysis (en)
http://linked.open.../riv/klicoveSlovo
http://linked.open...odStatuVydavatele
  • CZ - Česká republika
http://linked.open...ontrolniKodProRIV
  • [64C5C242BD7C]
http://linked.open...i/riv/nazevZdroje
  • Chemické listy
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http://linked.open...ichTvurcuVysledku
http://linked.open...cetTvurcuVysledku
http://linked.open...UplatneniVysledku
http://linked.open...v/svazekPeriodika
  • 104
http://linked.open...iv/tvurceVysledku
  • Kodíček, Milan
  • Jurga, Vojtěch
http://linked.open...ain/vavai/riv/wos
  • 000277072600004
http://linked.open...n/vavai/riv/zamer
issn
  • 0009-2770
number of pages
http://localhost/t...ganizacniJednotka
  • 22330
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