title: Detecting native folds in mixtures of proteins that contain disulfide bonds.
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.
authors.affiliation: Baker Laboratory of Chemistry and Chemical Biology, Cornell University, Ithaca, New York 14353-1301, USA. mnarayan@utep.edu
authors.forename: Mahesh
authors.initials: M
authors.lastname: Narayan
authors.forename: Ervin
authors.initials: E
authors.lastname: Welker
authors.forename: Huili
authors.initials: H
authors.lastname: Zhai
authors.forename: Xuemei
authors.initials: X
authors.lastname: Han
authors.forename: Guoqiang
authors.initials: G
authors.lastname: Xu
authors.forename: Fred W
authors.initials: FW
authors.lastname: McLafferty
authors.forename: Harold A
authors.initials: HA
authors.lastname: Scheraga
mesh_terms: D000465:Algorithms; D001665:Binding Sites; D045424:Complex Mixtures / Q000737:chemistry; D004220:Disulfides / Q000737:chemistry*; D010449:Peptide Mapping / Q000379:methods*; D011485:Protein Binding; D017510:Protein Folding; D011506:Proteins / Q000737:chemistry*; D021241:Spectrometry, Mass, Electrospray Ionization / Q000379:methods*; D017550:Spectroscopy, Fourier Transform Infrared / Q000379:methods*
chemical_list: D045424:Complex Mixtures; D004220:Disulfides; D011506:Proteins