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Thermal unfolding of the archaeal DNA and RNA binding protein Ssh10.
Biochem Biophys Res Commun. 2008 Sep 05; 373(4):482-7.BB

Abstract

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.

Authors+Show Affiliations

Medical Biochemistry and Biophysics, Karolinska Institutet, SE-171 77 Stockholm, Sweden.No affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info available

Pub Type(s)

Journal Article
Research Support, Non-U.S. Gov't

Language

eng

PubMed ID

18571501

Citation

Wu, Xiaoqiu, et al. "Thermal Unfolding of the Archaeal DNA and RNA Binding Protein Ssh10." Biochemical and Biophysical Research Communications, vol. 373, no. 4, 2008, pp. 482-7.
Wu X, Oppermann M, Berndt KD, et al. Thermal unfolding of the archaeal DNA and RNA binding protein Ssh10. Biochem Biophys Res Commun. 2008;373(4):482-7.
Wu, X., Oppermann, M., Berndt, K. D., Bergman, T., Jörnvall, H., Knapp, S., & Oppermann, U. (2008). Thermal unfolding of the archaeal DNA and RNA binding protein Ssh10. Biochemical and Biophysical Research Communications, 373(4), 482-7. https://doi.org/10.1016/j.bbrc.2008.06.030
Wu X, et al. Thermal Unfolding of the Archaeal DNA and RNA Binding Protein Ssh10. Biochem Biophys Res Commun. 2008 Sep 5;373(4):482-7. PubMed PMID: 18571501.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Thermal unfolding of the archaeal DNA and RNA binding protein Ssh10. AU - Wu,Xiaoqiu, AU - Oppermann,Madalina, AU - Berndt,Kurt D, AU - Bergman,Tomas, AU - Jörnvall,Hans, AU - Knapp,Stefan, AU - Oppermann,Udo, Y1 - 2008/06/20/ PY - 2008/06/05/received PY - 2008/06/06/accepted PY - 2008/6/24/pubmed PY - 2008/8/30/medline PY - 2008/6/24/entrez SP - 482 EP - 7 JF - Biochemical and biophysical research communications JO - Biochem Biophys Res Commun VL - 373 IS - 4 N2 - 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. SN - 1090-2104 UR - https://www.unboundmedicine.com/medline/citation/18571501/Thermal_unfolding_of_the_archaeal_DNA_and_RNA_binding_protein_Ssh10_ L2 - https://linkinghub.elsevier.com/retrieve/pii/S0006-291X(08)01161-3 DB - PRIME DP - Unbound Medicine ER -