Prediction of the three-dimensional structures of the biotinylated domain from yeast pyruvate carboxylase and of the lipoylated H-protein from the pea leaf glycine cleavage system: A new automated method for the prediction of protein tertiary structure
Author:
Funder
Science and Engineering Research Council
Publisher
Wiley
Subject
Molecular Biology,Biochemistry
Link
http://onlinelibrary.wiley.com/wol1/doi/10.1002/pro.5560020413/fullpdf
Reference37 articles.
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2. Cloning and sequence analysis of the genes encoding the dihydrolipoamide acetyltransferase and dihydrolipoamide dehydrogenase components of the pyruvate dehydrogenase multienzyme complex of Bacillus stearothermophilus;Borges;Eur. J. Biochem.,1990
3. The three-dimensional structure of the lipoyl domain from Bacillus stearothermophilus pyruvate dehydrogenase multienzyme complex;Dardel;J. Mol. Biol.,1993
4. Sequence-specific 1H NMR assignment and secondary structure of the lipoyl domain of the Bacillus stearothermophilus pyruvate dehydrogenase multienzyme complex;Dardel;Eur. J. Biochem.,1991
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