umu.sePublikationer
Ändra sökning
RefereraExporteraLänk till posten
Permanent länk

Direktlänk
Referera
Referensformat
  • apa
  • ieee
  • modern-language-association-8th-edition
  • vancouver
  • Annat format
Fler format
Språk
  • de-DE
  • en-GB
  • en-US
  • fi-FI
  • nn-NO
  • nn-NB
  • sv-SE
  • Annat språk
Fler språk
Utmatningsformat
  • html
  • text
  • asciidoc
  • rtf
Folding of an unfolded protein by macromolecular crowding in vitro
Umeå universitet, Teknisk-naturvetenskapliga fakulteten, Kemiska institutionen.
Umeå universitet, Teknisk-naturvetenskapliga fakulteten, Kemiska institutionen.
2014 (Engelska)Ingår i: Biochemistry, ISSN 0006-2960, E-ISSN 1520-4995, Vol. 53, nr 14, s. 2271-2277Artikel i tidskrift (Refereegranskat) Published
Abstract [en]

Protein folding in vivo takes place in a highly crowded environment. The resulting excluded volume forces are thought to stabilize folded forms of proteins. In agreement, many in vitro studies have shown that the presence of macromolecular crowding agents increases the stability of folded proteins but often by only a few kJ per mol. Although it should not matter at what position in the transition between folded and unfolded forms the effect of crowding is employed, there have been no studies assessing whether excluded volume forces alone can correctly fold polypeptides that are mostly unfolded. However, some studies have indicated that the effect of crowding becomes larger the more destabilized the protein is (but still being folded), suggesting that the crowding effect may be exaggerated for unfolded proteins. To address this question directly, we turned to a destabilized mutant of protein L that is mostly unfolded in water but can be folded upon addition of salt. We find that the effect of 200 mg/mL Dextran 20 on the folding equilibrium constant for unfolded protein L (ΔΔGU ≈ 2 kJ mol(-1)) matches the crowding effects found on the folded wild type protein and the mutant when prefolded by salt. This result indicates that the excluded volume effect is independent of starting protein stability and that crowding can shift the reaction toward the folded form when the polypeptide is in the transition region between folded and unfolded states.

Ort, förlag, år, upplaga, sidor
American Chemical Society (ACS), 2014. Vol. 53, nr 14, s. 2271-2277
Nyckelord [en]
adsorption, cellulose derivatives, surface interactions, surface modification, cellulose model surfaces, cellulose surfaces, initial adsorption, N-methylmorpholine-N-oxide, partial least squares models, polydispersity indices, regenerated cellulose, cellulose, least squares approximations, polydispersity, surface treatment, ultrathin films, molecular weight distribution
Nationell ämneskategori
Kemi Biokemi och molekylärbiologi
Identifikatorer
URN: urn:nbn:se:umu:diva-87819DOI: 10.1021/bi500222gISI: 000334657900009PubMedID: 24665900OAI: oai:DiVA.org:umu-87819DiVA, id: diva2:711637
Tillgänglig från: 2014-04-10 Skapad: 2014-04-10 Senast uppdaterad: 2018-06-08Bibliografiskt granskad

Open Access i DiVA

Fulltext saknas i DiVA

Övriga länkar

Förlagets fulltextPubMed

Personposter BETA

Ådén, JörgenWittung-Stafshede, Pernilla

Sök vidare i DiVA

Av författaren/redaktören
Ådén, JörgenWittung-Stafshede, Pernilla
Av organisationen
Kemiska institutionen
I samma tidskrift
Biochemistry
KemiBiokemi och molekylärbiologi

Sök vidare utanför DiVA

GoogleGoogle Scholar

doi
pubmed
urn-nbn

Altmetricpoäng

doi
pubmed
urn-nbn
Totalt: 434 träffar
RefereraExporteraLänk till posten
Permanent länk

Direktlänk
Referera
Referensformat
  • apa
  • ieee
  • modern-language-association-8th-edition
  • vancouver
  • Annat format
Fler format
Språk
  • de-DE
  • en-GB
  • en-US
  • fi-FI
  • nn-NO
  • nn-NB
  • sv-SE
  • Annat språk
Fler språk
Utmatningsformat
  • html
  • text
  • asciidoc
  • rtf