ArticleJournal of the American Society for Mass Spectrometry2007
Monitoring copopulated conformational states during protein folding events using electrospray ionization-ion mobility spectrometry-mass spectrometry.
Article in Journal of the American Society for Mass Spectrometry, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 50 papers.
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Who cites it
50 citing papers in PubMed.
- Elucidation of Dithiol-yne Comb Polymer Architectures by Tandem Mass Spectrometry and Ion Mobility Techniques.Polymers · 2024Article
- Mass Spectrometry Investigation of Some ATP-Binding Cassette (ABC) Proteins.Medicina (Kaunas, Lithuania) · 2024Review
- Are the Gas-Phase Structures of Molecular Elephants Enduring or Ephemeral? Results from Time-Dependent, Tandem Ion Mobility.Analytical chemistry · 2023Article
- Mass spectrometric insights into protein aggregation.Essays in biochemistry · 2023Review
- Mass Spectrometry Methods for Measuring Protein Stability.Chemical reviews · 2022Review
- Generating Ensembles of Dynamic Misfolding Proteins.Frontiers in neuroscience · 2022Review
- Utilizing Ion Mobility-Mass Spectrometry to Investigate the Unfolding Pathway of Cu/Zn Superoxide Dismutase.Frontiers in chemistry · 2021Article
- Following Structural Changes by Thermal Denaturation Using Trapped Ion Mobility Spectrometry-Mass Spectrometry.The journal of physical chemistry. B · 2020Article
- Conditions for Analysis of Native Protein Structures Using Uniform Field Drift Tube Ion Mobility Mass Spectrometry and Characterization of Stable Calibrants for TWIM-MS.Journal of the American Society for Mass Spectrometry · 2019Article
- A peptide-display protein scaffold to facilitate single molecule force studies of aggregation-prone peptides.Protein science : a publication of the Protein Society · 2018Article
- The Role of Mass Spectrometry in Structural Studies of Flavin-Based Electron Bifurcating Enzymes.Frontiers in microbiology · 2018Review
- pH Dependence of the Number of Discrete Conformers of Carbonic Anhydrase 2, as Evaluated from Collision Cross-Section Using Ion Mobility Coupled with Electrospray Ionization.Mass spectrometry (Tokyo, Japan) · 2018Article
- Native Mass Spectrometry: What is in the Name?Journal of the American Society for Mass Spectrometry · 2017Article
- Simultaneous analysis of enzyme structure and activity by kinetic capillary electrophoresis-MS.Nature chemical biology · 2016Article
- Towards the Analysis of High Molecular Weight Proteins and Protein complexes using TIMS-MS.International journal for ion mobility spectrometry : official publication of the International Society for Ion Mobility Spectrometry · 2016Article
- Systemic amyloidoses and proteomics: The state of the art.EuPA open proteomics · 2016Article
- Ion Mobility-Mass Spectrometry Analysis of Cross-Linked Intact Multiprotein Complexes: Enhanced Gas-Phase Stabilities and Altered Dissociation Pathways.Analytical chemistry · 2016Article
- Changes in protein structure monitored by use of gas-phase hydrogen/deuterium exchange.Proteomics · 2015Article
- The N-terminal residues 43 to 60 form the interface for dopamine mediated α-synuclein dimerisation.PloS one · 2015Article
- Characterization of polylactides with different stereoregularity using electrospray ionization ion mobility mass spectrometry.Journal of the American Society for Mass Spectrometry · 2014Article
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Authors and funding
5 authors.
Funding
Abstract
The precise mechanism of protein folding remains elusive and there is a deficiency of biophysical techniques that are capable of monitoring the individual behavior of copopulated protein conformers during the folding process. Herein, an ion mobility spectrometry (IMS) device integrated with electrospray ionization mass spectrometry (ESI-MS) has been used to successfully separate and analyze protein conformers differing in cross section and/or charge state. In an initial test, an ensemble of folded and partially folded conformers of the protein cytochrome c was separated. A detailed study undertaken on the amyloidogenic protein beta(2)-microglobulin (beta(2)m), which forms fibrils by protein unfolding followed by self-aggregation and is responsible for the disease dialysis-related amyloidosis, has generated important insights into its folding landscape. Initially, a systematic titration of beta(2)m over the pH range 2 to 7 using ESI-IMS-MS allowed individual conformers to be monitored and quantified throughout the acid denaturation process. Furthermore, a comparison of wild-type beta(2)m with single and double amino acid variants with a range of folding stabilities and propensities for amyloid fibril formation has provided illuminating evidence of the role of different conformers in protein stability and amyloidogenic aggregation. The ESI-IMS-MS data presented here not only demonstrate an important and informative further dimension to ESI-MS, but also illustrate the potential of the ESI-IMS-MS technique for unravelling protein folding enigmas in general and studying protein misfolding diseases in particular.
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