Mass spectrometric analysis of the rapamycin-dependent phosphorylation sites of the yeast protein kinase NPR1

Débora Bonenfant; Thierry Mini; Estela Jacinto; Tobias Schmelzle; Michael N. Hall; Paul Jenö

Mass spectrometric analysis of the rapamycin-dependent phosphorylation sites of the yeast protein kinase NPR1

Débora Bonenfant, Thierry Mini, Estela Jacinto, Tobias Schmelzle, Michael N. Hall, Paul Jenö

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

Abstract

The mass spectrometric analysis of the rapamycin-dependent phosphorylation sites of the yeast protein kinase NPR1 was described. The signal intensites of the pairs of nonphosphorylated and phosphorylated peptides were compared by electrospray ionization (ESI). It was revealed that three tryptic peptides T57, T63 and T68 from the regulatory domain were most heavily phosphorylated. The β-elimination with Ba(OH)₂ was used to facilitate the fragmentation process, due to strong inhibition of the fragmentation process caused by the presence of the phosphate group.

Original language	English (US)
Pages	315-316
Number of pages	2
State	Published - 2002
Externally published	Yes
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

All Science Journal Classification (ASJC) codes

Spectroscopy

Cite this

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title = "Mass spectrometric analysis of the rapamycin-dependent phosphorylation sites of the yeast protein kinase NPR1",

abstract = "The mass spectrometric analysis of the rapamycin-dependent phosphorylation sites of the yeast protein kinase NPR1 was described. The signal intensites of the pairs of nonphosphorylated and phosphorylated peptides were compared by electrospray ionization (ESI). It was revealed that three tryptic peptides T57, T63 and T68 from the regulatory domain were most heavily phosphorylated. The β-elimination with Ba(OH)2 was used to facilitate the fragmentation process, due to strong inhibition of the fragmentation process caused by the presence of the phosphate group.",

author = "D{\'e}bora Bonenfant and Thierry Mini and Estela Jacinto and Tobias Schmelzle and Hall, {Michael N.} and Paul Jen{\"o}",

year = "2002",

language = "English (US)",

pages = "315--316",

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

}

Mass spectrometric analysis of the rapamycin-dependent phosphorylation sites of the yeast protein kinase NPR1. / Bonenfant, Débora; Mini, Thierry; Jacinto, Estela et al.
2002. 315-316 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 - Mass spectrometric analysis of the rapamycin-dependent phosphorylation sites of the yeast protein kinase NPR1

AU - Bonenfant, Débora

AU - Mini, Thierry

AU - Jacinto, Estela

AU - Schmelzle, Tobias

AU - Hall, Michael N.

AU - Jenö, Paul

PY - 2002

Y1 - 2002

N2 - The mass spectrometric analysis of the rapamycin-dependent phosphorylation sites of the yeast protein kinase NPR1 was described. The signal intensites of the pairs of nonphosphorylated and phosphorylated peptides were compared by electrospray ionization (ESI). It was revealed that three tryptic peptides T57, T63 and T68 from the regulatory domain were most heavily phosphorylated. The β-elimination with Ba(OH)2 was used to facilitate the fragmentation process, due to strong inhibition of the fragmentation process caused by the presence of the phosphate group.

AB - The mass spectrometric analysis of the rapamycin-dependent phosphorylation sites of the yeast protein kinase NPR1 was described. The signal intensites of the pairs of nonphosphorylated and phosphorylated peptides were compared by electrospray ionization (ESI). It was revealed that three tryptic peptides T57, T63 and T68 from the regulatory domain were most heavily phosphorylated. The β-elimination with Ba(OH)2 was used to facilitate the fragmentation process, due to strong inhibition of the fragmentation process caused by the presence of the phosphate group.

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UR - http://www.scopus.com/inward/citedby.url?scp=2442699315&partnerID=8YFLogxK

M3 - Paper

AN - SCOPUS:2442699315

SP - 315

EP - 316

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

Y2 - 2 June 2002 through 6 June 2002

ER -

Mass spectrometric analysis of the rapamycin-dependent phosphorylation sites of the yeast protein kinase NPR1

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All Science Journal Classification (ASJC) codes

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