A diketoreductase exhibits unique renaturation profile from thermal-induced protein unfolding.
Proteins can refold from thermal-induced denaturation. Apo-diketoreductase exhibited a unique refolding profile, in which the degree of refolding from higher temperature was more complete. Partial aggregation and structural change may provide possible explanation on this phenomenon.
Laboratory of Chemical Biology, China Pharmaceutical University, 24 Tongjia Street, Nanjing, 210009, Jiangsu, People's Republic of China.
Meiling
M
Lu
Xu
X
Cao
Xin
X
Yang
Heng
H
Zheng
Nan
N
Liu
Yun
Y
Jiang
Donghai
D
Lin
Yijun
Y
Chen
D000150:Acinetobacter / Q000201:enzymology; D000429:Alcohol Oxidoreductases / Q000737:chemistry*; D001051:Apoenzymes / Q000737:chemistry; D004795:Enzyme Stability; D006358:Hot Temperature; D008958:Models, Molecular; D017510:Protein Folding; D020673:Protein Renaturation
D001051:Apoenzymes; D000429:Alcohol Oxidoreductases