Thermal unfolding of the archaeal DNA and RNA binding protein Ssh10.
|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 un ... [truncated at 450 characters in length]|
|Author||Wu, Xiaoqiu; Oppermann, Madalina; Berndt, Kurt D; et al|
|Subject||Amino Acid Sequence Archaeal Proteins Calorimetry, Differential Scanning Circular Dichroism DNA-Binding Proteins Histones Hot Temperature Hydrogen-Ion Concentration Molecular Sequence Data Protein Denaturation Protein Folding RNA-Binding Proteins Sulfolobus Thermodynamics chemistry metabolism chemistry metabolism chemistry metabolism chemistry metabolism metabolism|