Abstract
Flexible structures of intrinsically disordered proteins (IDPs) are crucial for versatile functions in living organisms, which involve interaction with diverse partners. Electrospray ionization ion mobility mass spectrometry (ESI-IM-MS) has been widely applied for structural characterization of apo-state and ligand-associated IDPs via two-dimensional separation in the gas phase. Gas-phase IDP structures have been regarded as kinetically trapped states originated from conformational features in solution. However, an implication of the states remains elusive in the structural characterization of IDPs, because it is unclear what structural property of IDPs is preserved. Recent studies have indicated that the conformational features of IDPs in solution are not fully reproduced in the gas phase. Nevertheless, the molecular interactions captured in the gas phase amplify the structural differences between IDP conformers. Therefore, an IDP conformational change that is not observed in solution is observable in the gas-phase structures obtained by ESI-IM-MS. Herein, we have presented up-to-date researches on the key implications of kinetically trapped states in the gas phase with a brief summary of the structural dynamics of IDPs in ESI-IM-MS.
| Original language | English |
|---|---|
| Journal | Mass Spectrometry Reviews |
| DOIs | |
| Publication status | Published - 2019 Jan 1 |
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Keywords
- electrospray ionization (ESI)
- intrinsically disordered protein
- ion mobility mass spectrometry (IM-MS)
- non-equilibrium state
- protein-ligand interaction
ASJC Scopus subject areas
- Analytical Chemistry
- Condensed Matter Physics
- Biochemistry, Genetics and Molecular Biology(all)
- Spectroscopy
Cite this
Gas-phase conformations of intrinsically disordered proteins and their complexes with ligands : Kinetically trapped states during transfer from solution to the gas phase. / Han, Jong Yoon; Choi, Tae Su; Heo, Chae Eun; Son, Myung Kook; Kim, Hugh I.
In: Mass Spectrometry Reviews, 01.01.2019.Research output: Contribution to journal › Review article
}
TY - JOUR
T1 - Gas-phase conformations of intrinsically disordered proteins and their complexes with ligands
T2 - Kinetically trapped states during transfer from solution to the gas phase
AU - Han, Jong Yoon
AU - Choi, Tae Su
AU - Heo, Chae Eun
AU - Son, Myung Kook
AU - Kim, Hugh I.
PY - 2019/1/1
Y1 - 2019/1/1
N2 - Flexible structures of intrinsically disordered proteins (IDPs) are crucial for versatile functions in living organisms, which involve interaction with diverse partners. Electrospray ionization ion mobility mass spectrometry (ESI-IM-MS) has been widely applied for structural characterization of apo-state and ligand-associated IDPs via two-dimensional separation in the gas phase. Gas-phase IDP structures have been regarded as kinetically trapped states originated from conformational features in solution. However, an implication of the states remains elusive in the structural characterization of IDPs, because it is unclear what structural property of IDPs is preserved. Recent studies have indicated that the conformational features of IDPs in solution are not fully reproduced in the gas phase. Nevertheless, the molecular interactions captured in the gas phase amplify the structural differences between IDP conformers. Therefore, an IDP conformational change that is not observed in solution is observable in the gas-phase structures obtained by ESI-IM-MS. Herein, we have presented up-to-date researches on the key implications of kinetically trapped states in the gas phase with a brief summary of the structural dynamics of IDPs in ESI-IM-MS.
AB - Flexible structures of intrinsically disordered proteins (IDPs) are crucial for versatile functions in living organisms, which involve interaction with diverse partners. Electrospray ionization ion mobility mass spectrometry (ESI-IM-MS) has been widely applied for structural characterization of apo-state and ligand-associated IDPs via two-dimensional separation in the gas phase. Gas-phase IDP structures have been regarded as kinetically trapped states originated from conformational features in solution. However, an implication of the states remains elusive in the structural characterization of IDPs, because it is unclear what structural property of IDPs is preserved. Recent studies have indicated that the conformational features of IDPs in solution are not fully reproduced in the gas phase. Nevertheless, the molecular interactions captured in the gas phase amplify the structural differences between IDP conformers. Therefore, an IDP conformational change that is not observed in solution is observable in the gas-phase structures obtained by ESI-IM-MS. Herein, we have presented up-to-date researches on the key implications of kinetically trapped states in the gas phase with a brief summary of the structural dynamics of IDPs in ESI-IM-MS.
KW - electrospray ionization (ESI)
KW - intrinsically disordered protein
KW - ion mobility mass spectrometry (IM-MS)
KW - non-equilibrium state
KW - protein-ligand interaction
UR - http://www.scopus.com/inward/record.url?scp=85065043870&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=85065043870&partnerID=8YFLogxK
U2 - 10.1002/mas.21596
DO - 10.1002/mas.21596
M3 - Review article
AN - SCOPUS:85065043870
JO - Mass Spectrometry Reviews
JF - Mass Spectrometry Reviews
SN - 0277-7037
ER -