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Purification, catalytic properties and thermostability of 3-isopropylmalate dehydrogenase from Escherichia coli.
Adjustment of conformational flexibility is a key event in the thermal adaptation of proteins.
Revision of the amino-acid sequence of 3-isopropylmalate dehydrogenase from Salmonella typhimurium by means of X-ray crystallography.
Crystal structures of Escherichia coli and Salmonella typhimurium 3-isopropylmalate dehydrogenase and comparison with their thermophilic counterpart from Thermus thermophilus.
Sequence and homology model of 3-isopropylmalate dehydrogenase from the psychrotrophic bacterium Vibrio sp. I5 suggest reasons for thermal instability.
A novel structural basis for membrane association of a protein: construction of a chimeric soluble mutant of (S)-mandelate dehydrogenase from Pseudomonas putida.
Expression, crystallization and preliminary crystallographic analysis of human carbonyl reductase.