Probing peptide/peptide interactions using H/D exchange, MS/MS and ESI-MS: Structure and metal ion binding of gramicidin dimer

Raghu Chitta; Don L. Rempel; Michael L. Gross

Probing peptide/peptide interactions using H/D exchange, MS/MS and ESI-MS: Structure and metal ion binding of gramicidin dimer

Raghu Chitta, Don L. Rempel, Michael L. Gross

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

Abstract

The use of H/D exchange, MS/MS and ESI-MS for determining the peptide/peptide interactions and structure and metal ion binding of gramicidin dimer were discussed. The H/D exchange was done by diluting a concentrated solution of gramicidin in the protonated solvent with the deuterated solvent and immediately injecting the solution into the mass spectrometer. It was observed that the stability of the metal-ion-bound dimer decreases with increasing ionic radius of the metal ion. It was suggested that the metal ion binds on the inside of the dimer in such a way that larger metal ions push apart the monomers, weakening the dimer.

Original language	English
Pages	227-228
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

Conference

Conference	Proceedings - 50th ASMS Conference on Mass Spectrometry and Allied Topics
Country/Territory	United States
City	Orlando, FL
Period	06/2/02 → 06/6/02

Cite this

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title = "Probing peptide/peptide interactions using H/D exchange, MS/MS and ESI-MS: Structure and metal ion binding of gramicidin dimer",

abstract = "The use of H/D exchange, MS/MS and ESI-MS for determining the peptide/peptide interactions and structure and metal ion binding of gramicidin dimer were discussed. The H/D exchange was done by diluting a concentrated solution of gramicidin in the protonated solvent with the deuterated solvent and immediately injecting the solution into the mass spectrometer. It was observed that the stability of the metal-ion-bound dimer decreases with increasing ionic radius of the metal ion. It was suggested that the metal ion binds on the inside of the dimer in such a way that larger metal ions push apart the monomers, weakening the dimer.",

author = "Raghu Chitta and Rempel, {Don L.} and Gross, {Michael L.}",

year = "2002",

language = "English",

pages = "227--228",

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

}

Probing peptide/peptide interactions using H/D exchange, MS/MS and ESI-MS: Structure and metal ion binding of gramicidin dimer. / Chitta, Raghu; Rempel, Don L.; Gross, Michael L.
2002. 227-228 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

TY - CONF

T1 - Probing peptide/peptide interactions using H/D exchange, MS/MS and ESI-MS

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

AU - Chitta, Raghu

AU - Rempel, Don L.

AU - Gross, Michael L.

PY - 2002

Y1 - 2002

N2 - The use of H/D exchange, MS/MS and ESI-MS for determining the peptide/peptide interactions and structure and metal ion binding of gramicidin dimer were discussed. The H/D exchange was done by diluting a concentrated solution of gramicidin in the protonated solvent with the deuterated solvent and immediately injecting the solution into the mass spectrometer. It was observed that the stability of the metal-ion-bound dimer decreases with increasing ionic radius of the metal ion. It was suggested that the metal ion binds on the inside of the dimer in such a way that larger metal ions push apart the monomers, weakening the dimer.

AB - The use of H/D exchange, MS/MS and ESI-MS for determining the peptide/peptide interactions and structure and metal ion binding of gramicidin dimer were discussed. The H/D exchange was done by diluting a concentrated solution of gramicidin in the protonated solvent with the deuterated solvent and immediately injecting the solution into the mass spectrometer. It was observed that the stability of the metal-ion-bound dimer decreases with increasing ionic radius of the metal ion. It was suggested that the metal ion binds on the inside of the dimer in such a way that larger metal ions push apart the monomers, weakening the dimer.

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M3 - Paper

AN - SCOPUS:2442696841

SP - 227

EP - 228

Y2 - 2 June 2002 through 6 June 2002

ER -

Probing peptide/peptide interactions using H/D exchange, MS/MS and ESI-MS: Structure and metal ion binding of gramicidin dimer

Abstract

Conference

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