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Biophysical characterization of recombinant proteins: a key to higher structural genomics success Vedadi M; Arrowsmith CH; Allali-Hassani A; Senisterra G; Wasney GAJ Struct Biol 2010[Oct]; 172 (1): 107-19Hundreds of genomes have been successfully sequenced to date, and the data are publicly available. At the same time, the advances in large-scale expression and purification of recombinant proteins have paved the way for structural genomics efforts. Frequently, however, little is known about newly expressed proteins calling for large-scale protein characterization to better understand their biochemical roles and to enable structure-function relationship studies. In the Structural Genomics Consortium (SGC), we have established a platform to characterize large numbers of purified proteins. This includes screening for ligands, enzyme assays, peptide arrays and peptide displacement in a 384-well format. In this review, we describe this platform in more detail and report on how our approach significantly increases the success rate for structure determination. Coupled with high-resolution X-ray crystallography and structure-guided methods, this platform can also be used toward the development of chemical probes through screening families of proteins against a variety of chemical series and focused chemical libraries.|Biophysical Phenomena[MESH]|Crystallography, X-Ray[MESH]|Genomics/*methods[MESH]|Humans[MESH]|Ligands[MESH]|Protein Binding[MESH]|Protein Interaction Mapping/methods[MESH]|Proteomics/*methods[MESH]|Recombinant Proteins/*chemistry/genetics/metabolism[MESH]|Structure-Activity Relationship[MESH] |
