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.
Lu
Meiling
M
Laboratory of Chemical Biology, China Pharmaceutical University, 24 Tongjia Street, Nanjing, 210009, Jiangsu, People's Republic of China.
Cao
Xu
X
Yang
Xin
X
Zheng
Heng
H
Liu
Nan
N
Jiang
Yun
Y
Lin
Donghai
D
Chen
Yijun
Y
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