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Evaluation of a Commercial TIMS-Q-TOF Platform for Native Mass Spectrometry.

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Title: Evaluation of a Commercial TIMS-Q-TOF Platform for Native Mass Spectrometry.
Authors: Panczyk, Erin M.1,2,3 (AUTHOR), Lin, Yu-Fu1,2 (AUTHOR), Harvey, Sophie R.1,2 (AUTHOR), Snyder, Dalton T.2 (AUTHOR), Liu, Fanny C.4 (AUTHOR), Ridgeway, Mark E.3 (AUTHOR), Park, Melvin A.3 (AUTHOR), Bleiholder, Christian4,5 (AUTHOR), Wysocki, Vicki H.1,2 (AUTHOR) wysocki.11@osu.edu
Source: Journal of the American Society for Mass Spectrometry. 7/3/2024, Vol. 35 Issue 7, p1394-1402. 9p.
Abstract: Mass-spectrometry based assays in structural biology studies measure either intact or digested proteins. Typically, different mass spectrometers are dedicated for such measurements: those optimized for rapid analysis of peptides or those designed for high molecular weight analysis. A commercial trapped ion mobility-quadrupole-time-of-flight (TIMS-Q-TOF) platform is widely utilized for proteomics and metabolomics, with ion mobility providing a separation dimension in addition to liquid chromatography. The ability to perform high-quality native mass spectrometry of protein complexes, however, remains largely uninvestigated. Here, we evaluate a commercial TIMS-Q-TOF platform for analyzing noncovalent protein complexes by utilizing the instrument's full range of ion mobility, MS, and MS/MS (both in-source activation and collision cell CID) capabilities. The TIMS analyzer is able to be tuned gently to yield collision cross sections of native-like complexes comparable to those previously reported on various instrument platforms. In-source activation and collision cell CID were robust for both small and large complexes. TIMS-CID was performed on protein complexes streptavidin (53 kDa), avidin (68 kDa), and cholera toxin B (CTB, 58 kDa). Complexes pyruvate kinase (237 kDa) and GroEL (801 kDa) were beyond the trapping capabilities of the commercial TIMS analyzer, but TOF mass spectra could be acquired. The presented results indicate that the commercial TIMS-Q-TOF platform can be used for both omics and native mass spectrometry applications; however, modifications to the commercial RF drivers for both the TIMS analyzer and quadrupole (currently limited to m/z 3000) are necessary to mobility analyze protein complexes greater than about 60 kDa. [ABSTRACT FROM AUTHOR]
Copyright of Journal of the American Society for Mass Spectrometry is the property of American Chemical Society and its content may not be copied or emailed to multiple sites without the copyright holder's express written permission. Additionally, content may not be used with any artificial intelligence tools or machine learning technologies. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract. (Copyright applies to all Abstracts.)
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  Data: Evaluation of a Commercial TIMS-Q-TOF Platform for Native Mass Spectrometry.
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  Data: <searchLink fieldCode="AR" term="%22Panczyk%2C+Erin+M%2E%22">Panczyk, Erin M.</searchLink><relatesTo>1,2,3</relatesTo> (AUTHOR)<br /><searchLink fieldCode="AR" term="%22Lin%2C+Yu-Fu%22">Lin, Yu-Fu</searchLink><relatesTo>1,2</relatesTo> (AUTHOR)<br /><searchLink fieldCode="AR" term="%22Harvey%2C+Sophie+R%2E%22">Harvey, Sophie R.</searchLink><relatesTo>1,2</relatesTo> (AUTHOR)<br /><searchLink fieldCode="AR" term="%22Snyder%2C+Dalton+T%2E%22">Snyder, Dalton T.</searchLink><relatesTo>2</relatesTo> (AUTHOR)<br /><searchLink fieldCode="AR" term="%22Liu%2C+Fanny+C%2E%22">Liu, Fanny C.</searchLink><relatesTo>4</relatesTo> (AUTHOR)<br /><searchLink fieldCode="AR" term="%22Ridgeway%2C+Mark+E%2E%22">Ridgeway, Mark E.</searchLink><relatesTo>3</relatesTo> (AUTHOR)<br /><searchLink fieldCode="AR" term="%22Park%2C+Melvin+A%2E%22">Park, Melvin A.</searchLink><relatesTo>3</relatesTo> (AUTHOR)<br /><searchLink fieldCode="AR" term="%22Bleiholder%2C+Christian%22">Bleiholder, Christian</searchLink><relatesTo>4,5</relatesTo> (AUTHOR)<br /><searchLink fieldCode="AR" term="%22Wysocki%2C+Vicki+H%2E%22">Wysocki, Vicki H.</searchLink><relatesTo>1,2</relatesTo> (AUTHOR)<i> wysocki.11@osu.edu</i>
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  Data: <searchLink fieldCode="JN" term="%22Journal+of+the+American+Society+for+Mass+Spectrometry%22">Journal of the American Society for Mass Spectrometry</searchLink>. 7/3/2024, Vol. 35 Issue 7, p1394-1402. 9p.
– Name: Abstract
  Label: Abstract
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  Data: Mass-spectrometry based assays in structural biology studies measure either intact or digested proteins. Typically, different mass spectrometers are dedicated for such measurements: those optimized for rapid analysis of peptides or those designed for high molecular weight analysis. A commercial trapped ion mobility-quadrupole-time-of-flight (TIMS-Q-TOF) platform is widely utilized for proteomics and metabolomics, with ion mobility providing a separation dimension in addition to liquid chromatography. The ability to perform high-quality native mass spectrometry of protein complexes, however, remains largely uninvestigated. Here, we evaluate a commercial TIMS-Q-TOF platform for analyzing noncovalent protein complexes by utilizing the instrument's full range of ion mobility, MS, and MS/MS (both in-source activation and collision cell CID) capabilities. The TIMS analyzer is able to be tuned gently to yield collision cross sections of native-like complexes comparable to those previously reported on various instrument platforms. In-source activation and collision cell CID were robust for both small and large complexes. TIMS-CID was performed on protein complexes streptavidin (53 kDa), avidin (68 kDa), and cholera toxin B (CTB, 58 kDa). Complexes pyruvate kinase (237 kDa) and GroEL (801 kDa) were beyond the trapping capabilities of the commercial TIMS analyzer, but TOF mass spectra could be acquired. The presented results indicate that the commercial TIMS-Q-TOF platform can be used for both omics and native mass spectrometry applications; however, modifications to the commercial RF drivers for both the TIMS analyzer and quadrupole (currently limited to m/z 3000) are necessary to mobility analyze protein complexes greater than about 60 kDa. [ABSTRACT FROM AUTHOR]
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  Data: <i>Copyright of Journal of the American Society for Mass Spectrometry is the property of American Chemical Society and its content may not be copied or emailed to multiple sites without the copyright holder's express written permission. Additionally, content may not be used with any artificial intelligence tools or machine learning technologies. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract.</i> (Copyright applies to all Abstracts.)
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        Value: 10.1021/jasms.3c00320
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        Text: English
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              Text: 7/3/2024
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