Characterizing the structures and folding of free proteins using 2-D gas-phase separations: observation of multiple unfolded conformers.

Characterizing the structures and folding of free proteins using 2-D gas-phase separations: observation of multiple unfolded conformers. Research Abstract Details 

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Characterizing the structures and folding of free proteins using 2-D gas-phase separations: observation of multiple unfolded conformers. Abstract Text:

Alexandre A Shvartsburg,Fumin Li,Keqi Tang,Richard D Smith,

Understanding the 3-D structure and dynamics of proteins and other biological macromolecules in various environments is among the central challenges of chemistry. Electrospray ionization can often transfer ions from solution to gas phase with only limited structural distortion, allowing their profiling using mass spectrometry and other gas-phase approaches. Ion mobility spectrometry (IMS) can separate and characterize macroion conformations with high sensitivity and speed. However, IMS separation power is generally insufficient for full resolution of major structural variants of protein ions and elucidation of their interconversion dynamics. Here we report characterization of macromolecular conformations using field asymmetric waveform IMS (FAIMS) coupled to conventional IMS in conjunction with mass spectrometry. The collisional heating of ions in the electrodynamic funnel trap between FAIMS and IMS stages enables investigating the structural evolution of particular isomeric precursors as a function of the intensity and duration of activation that can be varied over large ranges. These new capabilities are demonstrated for ubiquitin and cytochrome c, two common model proteins for structure and folding studies. For nearly all charge states, two-dimensional FAIMS/IMS separations distinguish many more conformations than either FAIMS or IMS alone, including some with very low abundance. For cytochrome c in high charge states, we find several abundant "unfolded" isomer series not distinguishable by IMS, possibly corresponding to different "string of beads" geometries. The unfolding of specific ubiquitin conformers selected by FAIMS has been studied by employing their heating in the FAIMS/IMS interface.

Characterizing the structures and folding of free proteins using 2-D gas-phase separations: observation of multiple unfolded conformers. Publishing Authors By Initials

AA Shvartsburg,F Li,K Tang,RD Smith,

For similar proteins: ubiquitins: ubiquitin research abstracts see: proteins: ubiquitins: ubiquitin research

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Characterizing the structures and folding of free proteins using 2-D gas-phase separations: observation of multiple unfolded conformers. Journal Published:

PUBLICATION TYPE: Research Support, U.S. Gov't,

Journal: Analytical chemistry

VOLUME: 78

Page Numbers: 3304-15

Journal Abbreviation: Anal. Chem.

ISSN: 0003-2700

DAY: 15

MONTH: May

YEAR: 2006

Characterizing the structures and folding of free proteins using 2-D gas-phase separations: observation of multiple unfolded conformers. Information

Number of References:

LANGUAGE: eng

NlmUniqueID: 370536

Characterizing the structures and folding of free proteins using 2-D gas-phase separations: observation of multiple unfolded conformers. Keywords Mesh Terms:

KEYWORDS: Ubiquitin

MESH TERMS: metabolism

Chemical & Substance for Abstract: Characterizing the structures and folding of free proteins using 2-D gas-phase separations: observation of multiple unfolded conformers. Information

Substance Name: Cytochromes c

Registry Number: 9007-43-6

Grant and Affiliation Information for Characterizing the structures and folding of free proteins using 2-D gas-phase separations: observation of multiple unfolded conformers.

AFFILIATION: Biological Sciences Division, Pacific Northwest National Laboratory, P.O. Box 999, Richland, WA 99352, USA.

Country: United States

AGENCY: United States NCRR

GRANT: RR 18522

ACRONYM: RR

MEDLINETA: Anal Chem

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