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

Research output: Contribution to conferencePaperpeer-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 languageEnglish (US)
Pages121-122
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
CountryUnited States
CityOrlando, FL
Period6/2/026/6/02

All Science Journal Classification (ASJC) codes

  • Spectroscopy

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