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Remarkably slow folding of a small protein.
Department of Biochemistry, Umeå University.
Department of Biochemistry, Umeå University.
Department of Biochemistry, Umeå University.
Department of Biochemistry, Umeå University.
1997 (English)In: FEBS Letters, ISSN 0014-5793, E-ISSN 1873-3468, Vol. 411, no 2-3, 359-364 p.Article in journal (Refereed) Published
Abstract [en]

Equilibrium denaturation of the 72 amino acid alpha/beta-protein MerP, by acid, guanidine hydrochloride, or temperature, is fully reversible and follows a two-state model in which only the native and unfolded states are populated. A cis-trans equilibrium around a proline peptide bond causes a heterogeneity of the unfolded state and gives rise to a slow- and a fast folding population. With a rate constant of 1.2 s(-1) for the major fast folding population, which has none of the common intrinsically slow steps, MerP is the slowest folding protein of this small size yet reported.

Place, publisher, year, edition, pages
1997. Vol. 411, no 2-3, 359-364 p.
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Natural Sciences
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URN: urn:nbn:se:liu:diva-45428DOI: 10.1016/S0014-5793(97)00730-8ISI: A1997XN02400041PubMedID: 9271236OAI: oai:DiVA.org:liu-45428DiVA: diva2:266290
Available from: 2009-10-10 Created: 2009-10-10 Last updated: 2017-12-13

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Brorsson, Ann-ChristinJonsson, Bengt Harald

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