A N L     PROTEIN MAPPING GROUP
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The Protein Mapping Group is part of a multidisciplinary team of biochemists, microbiologists, molecular biologists, and structural biologists within the Biosciences Division at Argonne National Laboratory (ANL). The Group uses two-dimensional gel electrophoresis (2DE) coupled with computerized image and data analysis to characterize normal protein expression and to detect altered protein expression in biological systems responding to environmental or pathological stresses. Changes in the abundance or position of proteins in the 2DE patterns that correlate with exogenous pressures suggest the involvement of those proteins in the biological response mechanism. Identification of such proteins by using peptide mass mapping provides markers of biological response as well as keys to biochemical mechanisms related to detoxification of harmful chemicals, cellular response to metabolic stress, and commitment to differentiation or programmed cell death. The efforts of the Protein Mapping Group are currently focused on analysis of proteins from microbial systems of interest to the U.S. Department of Energy. Data from prior studies of mouse and human cell systems are also available. This website is designed to interface protein expression data with genome sequence and metabolic pathway databases in order to place the observed fluctuations in protein expression into the context of the whole cell system. When publicly available, complete genome sequences are associated with the corresponding 2DE protein patterns. This site is comprised of several subsites connected through hyperlinks. The menu tabs at the top of each page are used to navigate to the subsites of interest and each subsite has a help menu describing the specific utilities available. For information regarding the software used to develop and maintain this website, please use the "Admin" button to contact the website administrator. Additional information regarding experimental protocols, data collection and analysis, and experimental results can be found under the "Methods" menu tab or in our publications.
 
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The deviation of measured MW and pI of identified proteines from the predicted values
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