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The “Two-State fold...
The “Two-State folder” MerP forms partially unfolded structures that show temperature dependent hydrogen exchange
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- Brorsson, Ann-Christin (author)
- Umeå universitet,Kemiska institutionen,Department of Biochemistry, Umeå University
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- Kjellson, Annika (author)
- Umeå universitet,Kemiska institutionen,Department of Biochemistry, Umeå University
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- Aronsson, Göran (author)
- Biopool, Umeå, Sweden,Biopool AB
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- Sethson, Ingmar (author)
- Umeå universitet,Kemiska institutionen,Department of Organic Chemistry, Umeå University
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- Hambraeus, Charlotta (author)
- University of Southern Stockholm, Center for Structural Biochemistry, Huddinge, Sweden
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- Jonsson, Bengt-Harald, 1949- (author)
- Linköpings universitet,Tekniska högskolan,Molekylär Bioteknik
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(creator_code:org_t)
- London : Academic Press, 2004
- 2004
- English.
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In: Journal of Molecular Biology. - London : Academic Press. - 0022-2836 .- 1089-8638. ; 340:2, s. 333-344
- Related links:
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https://urn.kb.se/re...
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https://doi.org/10.1...
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https://urn.kb.se/re...
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Abstract
Subject headings
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- We have analysed the folding energy landscape of the 72 amino acid protein MerP by monitoring native state hydrogen exchange as a function of temperature in the range of 7-55 degrees C. The temperature dependence of the hydrogen exchange has allowed us to determine DeltaG, DeltaH and DeltaC(p) values for the conformational processes that permit hydrogen exchange. When studied with the traditional probes, fluorescence and CD, MerP appears to behave as a typical two-state protein, but the results from the hydrogen exchange analysis reveal a much more complex energy landscape. Analysis at the individual amino acid level show that exchange is allowed from an ensemble of partially unfolded structures (i.e. intermediates) in which the stabilities at the amino acid level form a broad distribution throughout the protein. The formation of partially unfolded structures might contribute to the unusually slow folding of MerP.
Keyword
- protein folding
- hydrogen exchange
- protein stability
- intermediate
- partially unfolded
- NATURAL SCIENCES
Publication and Content Type
- ref (subject category)
- art (subject category)
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