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      Native Mass Spectrometry: Recent Progress and Remaining Challenges

      Author(s): 1 , 2 , 2 , 1 , 2 , 1 , 2
      Publication date Created:
      Publication date (Print):
      Journal: Annual Review of Biophysics
      Publisher: Annual Reviews

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          Abstract

          Native mass spectrometry (nMS) has emerged as an important tool in studying the structure and function of macromolecules and their complexes in the gas phase. In this review, we cover recent advances in nMS and related techniques including sample preparation, instrumentation, activation methods, and data analysis software. These advances have enabled nMS-based techniques to address a variety of challenging questions in structural biology. The second half of this review highlights recent applications of these technologies and surveys the classes of complexes that can be studied with nMS. Complementarity of nMS to existing structural biology techniques and current challenges in nMS are also addressed.

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          Most cited references178

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          Electrospray ionization for mass spectrometry of large biomolecules

          J Fenn, M. M. Mann, C. C. Meng … (1989)
          Article 0 comments Cited 760 times – based on 0 reviews     Review now
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            Bayesian deconvolution of mass and ion mobility spectra: from binary interactions to polydisperse ensembles.

            Michael T. Marty, Andrew J Baldwin, Erik Marklund … (2015)
            Interpretation of mass spectra is challenging because they report a ratio of two physical quantities, mass and charge, which may each have multiple components that overlap in m/z. Previous approaches to disentangling the two have focused on peak assignment or fitting. However, the former struggle with complex spectra, and the latter are generally computationally intensive and may require substantial manual intervention. We propose a new data analysis approach that employs a Bayesian framework to separate the mass and charge dimensions. On the basis of this approach, we developed UniDec (Universal Deconvolution), software that provides a rapid, robust, and flexible deconvolution of mass spectra and ion mobility-mass spectra with minimal user intervention. Incorporation of the charge-state distribution in the Bayesian prior probabilities provides separation of the m/z spectrum into its physical mass and charge components. We have evaluated our approach using systems of increasing complexity, enabling us to deduce lipid binding to membrane proteins, to probe the dynamics of subunit exchange reactions, and to characterize polydispersity in both protein assemblies and lipoprotein Nanodiscs. The general utility of our approach will greatly facilitate analysis of ion mobility and mass spectra.
            Article 0 comments Cited 312 times – based on 0 reviews     Review now
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              Analytical properties of the nanoelectrospray ion source.

              M Wilm, M. Männ (1996)
              The nanoelectrospray ion source (nanoES) has recently been developed and described theoretically. It is different from conventional electrospray sources and from other miniaturized electrospray sources by (i) its 1-2 microns spraying orifice achieved by pulling the spraying capillary to a fine tip, (ii) its very low flow rate of approximately 20 nL/min and the small size of droplets it generates, and (iii) the absence of solvent pumps and inlet valves. The fabrication and operation of nanoES needles is described in detail. Solutions with up to 0.1 M salt contents could be sprayed without sheath flow or pneumatic assist. Improved desolvation in nanoES led to instrument-limited resolution of the signals of a glycoprotein and the ability to signal average extensively allowed the C-terminal sequencing of a 40 kDa protein. Extensive mass spectrometric and tandem mass spectrometric investigation of the components of an unseparated peptide mixture was demonstrated by verification of 93% of the sequence of carbonic anhydrase. A rapid and robust desalting/concentration step coupled to the nanoES procedure allows the direct analysis of impure samples such as peptide mixtures extracted after in-gel digestion.
              Article 0 comments Cited 222 times – based on 0 reviews     Review now
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                Author and article information

                Journal
                Title: Annual Review of Biophysics
                Abbreviated Title: Annu. Rev. Biophys.
                Publisher: Annual Reviews
                ISSN (Print): 1936-122X
                ISSN (Electronic): 1936-1238
                Publication date Created: May 09 2022
                Publication date (Print): May 09 2022
                Volume: 51
                Issue: 1
                Pages: 157-179
                Affiliations
                [1 ]Department of Chemistry and Biochemistry, The Ohio State University, Columbus, Ohio, USA;
                [2 ]Resource for Native Mass Spectrometry Guided Structural Biology, The Ohio State University, Columbus, Ohio, USA
                Article
                DOI: 10.1146/annurev-biophys-092721-085421
                PubMed ID: 34982572
                SO-VID: 2c5f4f11-6ccc-47ba-b30d-26bb372a9003
                Copyright © © 2022
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