title: The molecular chaperone GroEL in complex with denatured proteins: increasing stability against temperature and trypsin action
metadata.name: dc.contributor.author
metadata.value: Marchenkov, Victor V.
metadata.lang: -
metadata.name: dc.contributor.author
metadata.value: Melnik, Tatiana N.
metadata.lang: -
metadata.name: dc.contributor.author
metadata.value: Marchenko, Natalia Yu.
metadata.lang: -
metadata.name: dc.contributor.author
metadata.value: Semisotnov, Gennady V.
metadata.lang: -
metadata.name: dc.date.accessioned
metadata.value: 2017-03-20T15:20:54Z
metadata.lang: -
metadata.name: dc.date.available
metadata.value: 2017-03-20T15:20:54Z
metadata.lang: -
metadata.name: dc.date.issued
metadata.value: 2016-12
metadata.lang: -
metadata.name: dc.identifier.other
metadata.value: 10.21638/11701/spbu04.2016.403
metadata.lang: -
metadata.name: dc.identifier.uri
metadata.value: http://hdl.handle.net/11701/6104
metadata.lang: -
metadata.name: dc.description.abstract
metadata.value: One of the functions of the Escherichia coli heat shock protein GroEL (HSP60) is its interaction
  with polypeptide chains lacking a rigid tertiary structure and prevention of their irreversible
  aggregation both in vivo and in vitro. Here we investigated the effect of denatured substrate
  proteins (lysozyme, pepsin and serum albumin) on GroEL structural stability against temperature
  (differential scanning microcalorimetry) and protease action (limited trypsinolysis). It was shown
  that the interaction with denatured proteins increases GroEL stability, the greater the molecular
  weight of denatured substrate proteins, the higher the GroEL stability. The results are important
  for understanding the mechanism of the substrate protein interaction with the chaperone and the
  principle of GroEL structural organization. Refs 22. Figs 2. Tables 1.
metadata.lang: en_GB
metadata.name: dc.description.sponsorship
metadata.value: Работа поддержана программой президиума РАН «Клеточная и молекулярная биология» (проект
  № 01201358029) и Российским научным фондом (грант РНФ № 14-24-00157).
metadata.lang: en_GB
metadata.name: dc.language.iso
metadata.value: ru
metadata.lang: en_GB
metadata.name: dc.publisher
metadata.value: St Petersburg State University
metadata.lang: en_GB
metadata.name: dc.relation.ispartofseries
metadata.value: Vestnik of St Petersburg University. Series 4. Physics. Chemistry;Vol. 3 (61); Issue 4
metadata.lang: -
metadata.name: dc.subject
metadata.value: heat shock proteins
metadata.lang: en_GB
metadata.name: dc.subject
metadata.value: GroEL chaperonin
metadata.lang: en_GB
metadata.name: dc.subject
metadata.value: protein-protein interactions
metadata.lang: en_GB
metadata.name: dc.subject
metadata.value: calorimetry
metadata.lang: en_GB
metadata.name: dc.subject
metadata.value: limited proteolysis
metadata.lang: en_GB
metadata.name: dc.title
metadata.value: The molecular chaperone GroEL in complex with denatured proteins: increasing stability against temperature and trypsin action
metadata.lang: en_GB
metadata.name: dc.type
metadata.value: Article
metadata.lang: en_GB
resources.filename: 03-Marchenko.pdf
resources.url: https://dspace.spbu.ru/bitstream/11701/6104/1/03-Marchenko.pdf
resources.format: Adobe PDF
resources.size: 488,91 kB