Brief Communications abstract
Nature Biotechnology 26, 427 - 429 (2008)
Published online: 17 February 2008 | doi:10.1038/nbt1380
Detecting native folds in mixtures of proteins that contain disulfide bonds
Mahesh Narayan1,2,5, Ervin Welker1,3,4,5, Huili Zhai1, Xuemei Han1, Guoqiang Xu1, Fred W McLafferty1 & Harold A Scheraga1
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.
- Baker Laboratory of Chemistry and Chemical Biology, Cornell University, Ithaca, New York 14353-1301, USA.
- Department of Chemistry, University of Texas at El Paso, El Paso, Texas 79968, USA.
- Institute of Biochemistry, Biological Research Centre of the Hungarian Academy, H-6701, Szeged, 62 Temesvari krt. Hungary.
- Institute of Enzymology, Biological Research Centre of the Hungarian Academy, H-1114, Budapest, 29 Karolina ut. Hungary.
- These authors contributed equally to this work.
Correspondence to: Mahesh Narayan1,2,5 e-mail: mnarayan@utep.edu
Correspondence to: Ervin Welker1,3,4,5 e-mail: welker@brc.hu.edu
Correspondence to: Harold A Scheraga1 e-mail: has5@cornell.edu
MORE ARTICLES LIKE THIS
These links to content published by NPG are automatically generated.
RESEARCH
Detecting native folds in mixtures of proteins that contain disulfide bondsNature Biotechnology Research (01 Apr 2008)
