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Refolding out of guanidine hydrochloride is an effective approach for high-throughput structural studies of small proteins.

Maxwell KL, Bona D, Liu C, Arrowsmith CH, Edwards AM,
Protein Science (2003) 12(9):2073-80 PublishedPSI:Phase 2  
Northeast Structural Genomics Consortium

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Low in vivo solubility of recombinant proteins expressed in Escherichia coli can seriously hinder the purification of structural samples for large-scale proteomic NMR and X-ray crystallography studies. ...
metabolism isolation & purification chemistry methods 
Crystallography, X-Ray Recombinant Proteins Proteome Escherichia coli Magnetic Resonance Spectroscopy Circular Dichroism Protein Conformation Biophysical Phenomena Guanidine Proteomics Protein Denaturation Protein Folding Electrophoresis, Polyacrylamide Gel Proteins Biophysics 
12931005  
10.1110/ps.0393503  
19 (Last update: 08/19/2017 11:16:43am)  
method  
Protein Sci. 2003 Sep;12(9):2073-80.