Detecting native folds in mixtures of proteins that contain disulfide bonds
Mahesh Narayan1, Ervin Welker, Huili Zhai
1Baker Laboratory of Chemistry and Chemical Biology, Cornell University, Ithaca, New York 14353-1301, USA. mnarayan@utep.edu
Abstract:
High-throughput in vitro refolding of proteins that contain disulfide bonds, for which soluble expression is particularly difficult, is severely impeded by the absence of effective methods for detecting their native forms. We demonstrate such a method, which combines mass spectrometry with mild reductions, requires no prior experimentation or knowledge of proteins' physicochemical characteristics, function or activity, and is amenable to automation. These are necessary criteria for structural genomics and proteomics applications.
Related Concept Videos
Protein Folding
Protein Structure Is Critical to Its Biological Function
Proteins perform a wide range of biological functions such as catalyzing chemical reactions, providing...
Protein Folding
Protein Folding Quality Check in the RER


