Thermal Analysis of a Mixture of Ribosomal Proteins by vT-ESI-MS: Toward a Parallel Approach for Characterizing the Stabilitome.
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The thermal stabilities of endogenous, intact proteins and protein assemblies in complex mixtures were characterized in parallel by means of variable-temperature electrospray ionization coupled to mass spectrometry (vT-ESI-MS). The method is demonstrated by directly measuring the melting transitions of seven proteins from a mixture of proteins derived from ribosomes. A proof-of-concept measurement of a fraction of an Escherichia coli lysate is provided to extend this approach to characterize the thermal stability of a proteome. As the solution temperature is increased, proteins and protein complexes undergo structural and organizational transitions; for each species, the folded unfolded and assembled disassembled populations are monitored based on changes in vT-ESI-MS charge state distributions and masses. The robustness of the approach illustrates a step toward the proteome-wide characterization of thermal stabilities and structural transitions-the stabilitome.
El-Baba, T. J., Raab, S. A., Buckley, R. P., Brown, C. J., Lutomski, C. A., Henderson, L. W., ... Clemmer, D. E.
complete list of authors
El-Baba, Tarick J||Raab, Shannon A||Buckley, Rachel P||Brown, Christopher J||Lutomski, Corinne A||Henderson, Lucas W||Woodall, Daniel W||Shen, Jiangchuan||Trinidad, Jonathan C||Niu, Hengyao||Jarrold, Martin F||Russell, David H||Laganowsky, Arthur||Clemmer, David E