Selective staining of proteins with hydrophobic surface sites on a native electrophoretic gel.
Chemical proteomics aims to characterize all of the proteins in the proteome with respect to their function, which is associated with their interaction with other molecules. We propose the identification of a subproteomic library of expressed proteins whose native structures are typified by the presence of hydrophobic surface sites, which are often involved in interactions with small molecules, membrane lipids, and other proteins, pertaining to their functions. We demonstrate that soluble globular proteins with hydrophobic surface sites can be detected selectively by staining on an electrophoretic gel run under nondenaturing conditions. The application of these staining techniques may help elucidate new catalytic, transport, and regulatory functionalities in complex proteomic screenings.
Department of Chemistry, University of Illinois at Chicago, 845 West Taylor Street, Suite 4500, Chicago, Illinois 60607, USA.
Martina
M
Bertsch
Richard J
RJ
Kassner
D001426:Bacterial Proteins / Q000378:metabolism; D001978:Bromphenol Blue / Q000378:metabolism; D002844:Chromatium / Q000378:metabolism; D004396:Coloring Agents / Q000378:metabolism; D045304:Cytochromes c / Q000378:metabolism; D015180:Electrophoresis, Gel, Two-Dimensional / Q000379:methods*; D004591:Electrophoresis, Polyacrylamide Gel / Q000379:methods; D006863:Hydrogen-Ion Concentration; D057927:Hydrophobic and Hydrophilic Interactions; D008563:Membrane Lipids / Q000378:metabolism; D011506:Proteins / Q000737:chemistry / Q000302:isolation & purification / Q000378:metabolism*; D040901:Proteomics / Q000379:methods*; D012680:Sensitivity and Specificity; D012995:Solubility; D013194:Staining and Labeling / Q000379:methods*; D016482:Urinalysis
D001426:Bacterial Proteins; D004396:Coloring Agents; D008563:Membrane Lipids; D011506:Proteins; D001978:Bromphenol Blue; D045304:Cytochromes c