Dynamics of Protein Kinase A and Anchoring Protein using enhanced hydrogen/Deuterium Exchange Mass Spectrometry (DXMS)

Yoshitomo Hamuro; Lora L. Burns; Kerri Zawadzski; Ganesh Anand; Jack S. Kim; Susan S. Taylor; Virgil L. Woods

Dynamics of Protein Kinase A and Anchoring Protein using enhanced hydrogen/Deuterium Exchange Mass Spectrometry (DXMS)

Yoshitomo Hamuro, Lora L. Burns, Kerri Zawadzski, Ganesh Anand, Jack S. Kim, Susan S. Taylor, Virgil L. Woods

Chemistry

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

Abstract

Deuterium exchange mass spectrometry (DXMS) was used to study the dynamics of Protein Kinase A and anchoring protein. The dynamics of PKA was also described by analyzing the hydrogen/deuterium (H/D) exchange pattern of cAMP-bound R and that of catalytic subunit (C)-bound R (R ₂C ₂ holo enzyme). It was found that proteolysis of the labeled protein generated a series of overlapping peptides covering over 99% of the protein primary sequence and the high peptide coverage enabled the study of the dynamics of whole protein. The interaction between the dimerization/docking (D/D) domain of PKA R and RPP8, which included the PKA kinase binding (AKB) domain of anchoring protein (D-AKAP2) was also described.

Original language	English (US)
Pages	121-122
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

All Science Journal Classification (ASJC) codes

Spectroscopy

Cite this

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title = "Dynamics of Protein Kinase A and Anchoring Protein using enhanced hydrogen/Deuterium Exchange Mass Spectrometry (DXMS)",

abstract = "Deuterium exchange mass spectrometry (DXMS) was used to study the dynamics of Protein Kinase A and anchoring protein. The dynamics of PKA was also described by analyzing the hydrogen/deuterium (H/D) exchange pattern of cAMP-bound R and that of catalytic subunit (C)-bound R (R 2C 2 holo enzyme). It was found that proteolysis of the labeled protein generated a series of overlapping peptides covering over 99% of the protein primary sequence and the high peptide coverage enabled the study of the dynamics of whole protein. The interaction between the dimerization/docking (D/D) domain of PKA R and RPP8, which included the PKA kinase binding (AKB) domain of anchoring protein (D-AKAP2) was also described.",

author = "Yoshitomo Hamuro and Burns, {Lora L.} and Kerri Zawadzski and Ganesh Anand and Kim, {Jack S.} and Taylor, {Susan S.} and Woods, {Virgil L.}",

year = "2002",

language = "English (US)",

pages = "121--122",

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Dynamics of Protein Kinase A and Anchoring Protein using enhanced hydrogen/Deuterium Exchange Mass Spectrometry (DXMS). / Hamuro, Yoshitomo; Burns, Lora L.; Zawadzski, Kerri et al.
2002. 121-122 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 - Dynamics of Protein Kinase A and Anchoring Protein using enhanced hydrogen/Deuterium Exchange Mass Spectrometry (DXMS)

AU - Hamuro, Yoshitomo

AU - Burns, Lora L.

AU - Zawadzski, Kerri

AU - Anand, Ganesh

AU - Kim, Jack S.

AU - Taylor, Susan S.

AU - Woods, Virgil L.

PY - 2002

Y1 - 2002

N2 - Deuterium exchange mass spectrometry (DXMS) was used to study the dynamics of Protein Kinase A and anchoring protein. The dynamics of PKA was also described by analyzing the hydrogen/deuterium (H/D) exchange pattern of cAMP-bound R and that of catalytic subunit (C)-bound R (R 2C 2 holo enzyme). It was found that proteolysis of the labeled protein generated a series of overlapping peptides covering over 99% of the protein primary sequence and the high peptide coverage enabled the study of the dynamics of whole protein. The interaction between the dimerization/docking (D/D) domain of PKA R and RPP8, which included the PKA kinase binding (AKB) domain of anchoring protein (D-AKAP2) was also described.

AB - Deuterium exchange mass spectrometry (DXMS) was used to study the dynamics of Protein Kinase A and anchoring protein. The dynamics of PKA was also described by analyzing the hydrogen/deuterium (H/D) exchange pattern of cAMP-bound R and that of catalytic subunit (C)-bound R (R 2C 2 holo enzyme). It was found that proteolysis of the labeled protein generated a series of overlapping peptides covering over 99% of the protein primary sequence and the high peptide coverage enabled the study of the dynamics of whole protein. The interaction between the dimerization/docking (D/D) domain of PKA R and RPP8, which included the PKA kinase binding (AKB) domain of anchoring protein (D-AKAP2) was also described.

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M3 - Paper

AN - SCOPUS:2442714150

SP - 121

EP - 122

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

Y2 - 2 June 2002 through 6 June 2002

ER -

Dynamics of Protein Kinase A and Anchoring Protein using enhanced hydrogen/Deuterium Exchange Mass Spectrometry (DXMS)

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