View publication

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

(click to unfold)
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 chemistry methods isolation & purification 
Crystallography, X-Ray Proteins Escherichia coli Proteomics Protein Conformation Protein Folding Recombinant Proteins Circular Dichroism Magnetic Resonance Spectroscopy Proteome Electrophoresis, Polyacrylamide Gel Biophysical Phenomena Biophysics Protein Denaturation Guanidine 
12931005  
10.1110/ps.0393503  
26 (Last update: 11/10/2018 1:20:48pm)  
method  
Protein Sci. 2003 Sep;12(9):2073-80.