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Thermal unfolding o...
Thermal unfolding of the archaeal DNA and RNA binding protein Ssh10
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Wu, X (author)
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Oppermann, M (author)
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- Berndt, Kurt D (author)
- Karolinska Institutet
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- Bergman, T (author)
- Karolinska Institutet
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- Jörnvall, H (author)
- Karolinska Institutet
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Knapp, S (author)
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Oppermann, U (author)
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(creator_code:org_t)
- Elsevier BV, 2008
- 2008
- English.
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In: Biochemical and Biophysical Research Communications - BBRC. - : Elsevier BV. - 0006-291X .- 1090-2104. ; 373:4, s. 482-487
- Related links:
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https://urn.kb.se/re...
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https://doi.org/10.1...
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Abstract
Subject headings
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- The reversible thermal unfolding of the archaeal histone-like protein Ssh10b from the extremophile Sulfolobus shibatae was studied using differential scanning calorimetry and circular dichroism spectroscopy. Analytical ultracentrifugation and gel filtration showed that Ssh10b is a stable dimer in the pH range 2.5-7.0. Thermal denaturation data fit into a two-state unfolding model, suggesting that the Ssh10 dimer unfolds as a single cooperative unit with a maximal melting temperature of 99.9 degrees C and an enthalpy change of 134 kcal/mol at pH 7.0. The heat capacity change upon unfolding determined from linear fits of the temperature dependence of DeltaH(cal) is 2.55 kcal/(mol K). The low specific heat capacity change of 13 cal/(mol K residue) leads to a considerable flattening of the protein stability curve (DeltaG (T)) and results in a maximal DeltaG of only 9.5 kcal/mol at 320 K and a DeltaG of only 6.0 kcal/mol at the optimal growth temperature of Sulfolobus.
Subject headings
- NATURVETENSKAP -- Biologi -- Biokemi och molekylärbiologi (hsv//swe)
- NATURAL SCIENCES -- Biological Sciences -- Biochemistry and Molecular Biology (hsv//eng)
Keyword
- *Hot Temperature
- Amino Acid Sequence
- Archaeal Proteins/chemistry/*metabolism
- Calorimetry
- Differential Scanning
- Circular Dichroism
- DNA-Binding Proteins/chemistry/*metabolism
- Histones/chemistry/*metabolism
- Hydrogen-Ion Concentration
- Molecular Sequence Data
- Protein Denaturation
- Protein Folding
- RNA-Binding Proteins/chemistry/*metabolism
- Sulfolobus/*metabolism
- Thermodynamics
- Other research area
- Annat forskningsområde
Publication and Content Type
- ref (subject category)
- art (subject category)
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