Probing the conformation difference between Ca 2+-ATP-actin and Mg 2+-ATP-actin by hydroxyl radicals and mass spectrometry

Jing Qu Guan, Steve C. Almo, Mark R. Chance

Research output: Contribution to conferencePaperpeer-review

Abstract

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.

Original languageEnglish (US)
Pages275-276
Number of pages2
StatePublished - 2002
EventProceedings - 50th ASMS Conference on Mass Spectrometry and Allied Topics - Orlando, FL, United States
Duration: Jun 2 2002Jun 6 2002

Other

OtherProceedings - 50th ASMS Conference on Mass Spectrometry and Allied Topics
Country/TerritoryUnited States
CityOrlando, FL
Period6/2/026/6/02

ASJC Scopus subject areas

  • Spectroscopy

Fingerprint

Dive into the research topics of 'Probing the conformation difference between Ca <sup>2+</sup>-ATP-actin and Mg <sup>2+</sup>-ATP-actin by hydroxyl radicals and mass spectrometry'. Together they form a unique fingerprint.

Cite this