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|
Thermolability of mutant MMACHC protein in the vitamin B12-responsive cblC disorder.
|Abstract||Methylmalonic aciduria and homocystinuria, cblC type, is the most common inborn error of cellular vitamin B12 metabolism. We previously showed that the protein carrying the mutation responsible for late-onset cblC (MMACHC-R161Q), treatable with high dose OHCbl, is able to bind OHCbl with wild-type affinity, leaving undetermined the disease mechanism involved [Froese et al., Mechanism of responsiveness, Mol. Genet. Metab. (2009).]. To assess wheth ... [truncated at 450 characters in length]|
|Author||Froese, D S; Healy, S; McDonald, M; et al|
|Subject||Age of Onset Amino Acid Metabolism, Inborn Errors Carrier Proteins Cobamides Fluorometry Homocystinuria Hot Temperature Humans Methylmalonic Acid Protein Denaturation Protein Stability Vitamin B 12 drug therapy genetics chemistry genetics chemistry drug therapy genetics urine analogs and derivatives chemistry genetics therapeutic use|