title: Method of protein stabilization based on prediction of intrinsically disordered regions. Stabilization of protein Gαo
metadata.name: dc.contributor.author
metadata.value: Nagibina, Galina S.
metadata.lang: -
metadata.name: dc.contributor.author
metadata.value: Dzhus, Uliana F.
metadata.lang: -
metadata.name: dc.contributor.author
metadata.value: Glukhov, Anatoly S.
metadata.lang: -
metadata.name: dc.contributor.author
metadata.value: Melnik, Tatiana N.
metadata.lang: -
metadata.name: dc.contributor.author
metadata.value: Melnik, Bogdan S.
metadata.lang: -
metadata.name: dc.date.accessioned
metadata.value: 2017-01-05T13:15:01Z
metadata.lang: -
metadata.name: dc.date.available
metadata.value: 2017-01-05T13:15:01Z
metadata.lang: -
metadata.name: dc.date.issued
metadata.value: 2016-09
metadata.lang: -
metadata.name: dc.identifier.other
metadata.value: 10.21638/11701/spbu04.2016.305
metadata.lang: -
metadata.name: dc.identifier.uri
metadata.value: http://hdl.handle.net/11701/5868
metadata.lang: -
metadata.name: dc.description.abstract
metadata.value: Protein Gαo from Drosophila melanogaster has been studied. We have designed an SS-bridge
  in this protein in such a way that its stability could be increased. The choice of a region in the
  polypeptide chain for insertion of the cysteine bridge was based on calculations performed using
  programs for the prediction of intrinsically disordered proteins. In our previous paper we proposed
  that, in structured proteins, these programs predict “weakened” protein regions unable to have
  a rigid structure without additional hydrophobic interactions rather than intrinsically disordered
  regions. Consequently, insertion of SS-bridges in such regions will most probably lead to stabilization
  of the protein. It was just this approach that was used in the presented study. It is demonstrated
  with the microcalorimetry method that the insertion of the designed SS-bridge resulted in
  4 K increase in the melting temperature of one domain of protein Gαo. Refs 20. Figs 3. Tables 1.
metadata.lang: en_GB
metadata.name: dc.description.sponsorship
metadata.value: Работа поддержана Российским научным фондом (грант РНФ N14-24-00157).
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 3
metadata.lang: -
metadata.name: dc.subject
metadata.value: Gαo
metadata.lang: en_GB
metadata.name: dc.subject
metadata.value: differential scanning microcalorimetry
metadata.lang: en_GB
metadata.name: dc.subject
metadata.value: SS-bridge
metadata.lang: en_GB
metadata.name: dc.subject
metadata.value: protein stability
metadata.lang: en_GB
metadata.name: dc.subject
metadata.value: protein intrinsic disorder
metadata.lang: en_GB
metadata.name: dc.title
metadata.value: Method of protein stabilization based on prediction of intrinsically disordered regions. Stabilization of protein Gαo
metadata.lang: en_GB
metadata.name: dc.type
metadata.value: Article
metadata.lang: en_GB
resources.filename: 05-Nagibina.pdf
resources.url: https://dspace.spbu.ru/bitstream/11701/5868/1/05-Nagibina.pdf
resources.format: Adobe PDF
resources.size: 851,46 kB