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

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

Biochemistry

Research output: Contribution to conference › Paper › peer-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 language	English (US)
Pages	275-276
Number of pages	2
State	Published - 2002
Event	Proceedings - 50th ASMS Conference on Mass Spectrometry and Allied Topics - Orlando, FL, United States Duration: Jun 2 2002 → Jun 6 2002

Other

Other	Proceedings - 50th ASMS Conference on Mass Spectrometry and Allied Topics
Country/Territory	United States
City	Orlando, FL
Period	6/2/02 → 6/6/02

ASJC Scopus subject areas

Spectroscopy

Cite this

Probing the conformation difference between Ca ²⁺-ATP-actin and Mg ²⁺-ATP-actin by hydroxyl radicals and mass spectrometry. / Guan, Jing Qu; Almo, Steve C.; Chance, Mark R.
2002. 275-276 Paper presented at Proceedings - 50th ASMS Conference on Mass Spectrometry and Allied Topics, Orlando, FL, United States.

Research output: Contribution to conference › Paper › peer-review

@conference{6e0a4a925af7474b80e963ff7628e21f,

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

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.",

author = "Guan, {Jing Qu} and Almo, {Steve C.} and Chance, {Mark R.}",

year = "2002",

language = "English (US)",

pages = "275--276",

note = "Proceedings - 50th ASMS Conference on Mass Spectrometry and Allied Topics ; Conference date: 02-06-2002 Through 06-06-2002",

}

TY - CONF

T1 - Probing the conformation difference between Ca 2+-ATP-actin and Mg 2+-ATP-actin by hydroxyl radicals and mass spectrometry

AU - Guan, Jing Qu

AU - Almo, Steve C.

AU - Chance, Mark R.

PY - 2002

Y1 - 2002

N2 - 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.

AB - 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.

UR - http://www.scopus.com/inward/record.url?scp=2442685807&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=2442685807&partnerID=8YFLogxK

M3 - Paper

AN - SCOPUS:2442685807

SP - 275

EP - 276

T2 - Proceedings - 50th ASMS Conference on Mass Spectrometry and Allied Topics

Y2 - 2 June 2002 through 6 June 2002

ER -

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

Abstract

Other

ASJC Scopus subject areas

Other files and links

Fingerprint

Cite this