The conformational differences between Ca 2+-ATP--actin and Mg 2+-ATP-G-actin probed by hydroxyl radicals and mass spectrometry (MS) were analyzed. Hydroxyl radicals generated by synchrotron x-rays probed the solvent accessibilities of discrete residues of a protein by forming a covalent adduct with a side chain. The solvent accessibilities were measured in terms of modification rates quantitated by MS, and the modified sites were identified by MS/MS. The conformational change of the protein was found to be correlated with the solvent accessibility variation of residues.
|Number of pages
|Published - 2002
|Proceedings - 50th ASMS Conference on Mass Spectrometry and Allied Topics - Orlando, FL, United States
Duration: Jun 2 2002 → Jun 6 2002
|Proceedings - 50th ASMS Conference on Mass Spectrometry and Allied Topics
|6/2/02 → 6/6/02
ASJC Scopus subject areas