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Folding of the αΙΙ-spectrin SH3 domain under physiological salt conditions
Umeå universitet, Medicinska fakulteten, Institutionen för medicinsk kemi och biofysik.
Umeå universitet, Teknisk-naturvetenskapliga fakulteten, Umeå centrum för molekylär patogenes (UCMP) (Teknisk-naturvetenskaplig fakultet).
Umeå universitet, Teknisk-naturvetenskapliga fakulteten, Kemiska institutionen.
2008 (Engelska)Ingår i: Archives of Biochemistry and Biophysics, ISSN 0003-9861, E-ISSN 1096-0384, Vol. 474, nr 1, s. 39-47Artikel i tidskrift (Refereegranskat) Published
Abstract [en]

The SH3 domain has often been used as a model for protein folding due to its typical two-state behaviour. However, recent experimental data at low pH as well as molecular dynamic simulations have indicated that the folding process of SH3 probably is more complicated, and may involve intermediate states. Using both kinetic and equilibrium measurements we have obtained evidence that under native-like conditions the folding of the spectrin SH3 domain does not follow a classic two-state behaviour. The curvature we observed in the Chevron plots is a strong indication of a non-linear activation energy relationship due to the presence of high-energy intermediates. In addition, circular dichroism measurements indicated that refolding after thermal denaturation did not follow the same pattern as thermal unfolding but rather implied less cooperativity and that the refolding transition increased with increasing protein concentration. Further, NMR experiments indicated that upon refolding the SH3 domain gave rise to more than one conformation. Therefore, our results suggest that the folding of the SH3 domain of II-spectrin does not follow a classical two-state process under high-salt conditions and neutral pH. Heterogeneous folding pathways, which can include folding intermediates as well as misfolded intermediates, might give a more reasonable insight into the folding behaviour of the II-spectrin SH3 domain.

Ort, förlag, år, upplaga, sidor
Elsevier, 2008. Vol. 474, nr 1, s. 39-47
Nyckelord [en]
SH3, Spectrin, Protein folding, NMR
Nationell ämneskategori
Biokemi och molekylärbiologi
Identifikatorer
URN: urn:nbn:se:umu:diva-9359DOI: 10.1016/j.abb.2008.02.042ISI: 000256459800006PubMedID: 18358826OAI: oai:DiVA.org:umu-9359DiVA, id: diva2:149030
Tillgänglig från: 2008-05-27 Skapad: 2008-05-27 Senast uppdaterad: 2019-08-07Bibliografiskt granskad

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Petzold, KatjaÖhman, AndersBackman, Lars

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Petzold, KatjaÖhman, AndersBackman, Lars
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Institutionen för medicinsk kemi och biofysikUmeå centrum för molekylär patogenes (UCMP) (Teknisk-naturvetenskaplig fakultet)Kemiska institutionen
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Archives of Biochemistry and Biophysics
Biokemi och molekylärbiologi

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