2022
DOI: 10.1038/s41570-021-00353-7
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Studying protein structure and function by native separation–mass spectrometry

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Cited by 42 publications
(39 citation statements)
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“…The ability to generate gas-phase protein ions using electrospray ionization (ESI) has placed mass spectrometry (MS) in the league of complementary techniques that enable characterization of protein structure and function. ESI is a soft ionization technique that transfers proteins from the solution phase to the gas phase while preserving the solution-phase structure of the protein to a great extent. The characteristic peaks in the ESI mass spectrum, related to multiply charged ions of intact protein, reveal many details about the tertiary structure of the macromolecule. , In general, a protein molecule in a folded state acquires fewer charges than in an unfolded state . Therefore, the factors affecting protein conformationsuch as pH, temperature, and solvent polarityare commonly altered to study protein folding dynamics with ESI-MS.…”
mentioning
confidence: 99%
“…The ability to generate gas-phase protein ions using electrospray ionization (ESI) has placed mass spectrometry (MS) in the league of complementary techniques that enable characterization of protein structure and function. ESI is a soft ionization technique that transfers proteins from the solution phase to the gas phase while preserving the solution-phase structure of the protein to a great extent. The characteristic peaks in the ESI mass spectrum, related to multiply charged ions of intact protein, reveal many details about the tertiary structure of the macromolecule. , In general, a protein molecule in a folded state acquires fewer charges than in an unfolded state . Therefore, the factors affecting protein conformationsuch as pH, temperature, and solvent polarityare commonly altered to study protein folding dynamics with ESI-MS.…”
mentioning
confidence: 99%
“…Not only the separation columns should be improved, but also novel separation modes should be developed. For better understanding of proteins’ functions, protein complexes have been studied via top-down native MS. 205 Nowadays, the separation of protein complexes under native conditions could be performed via SEC or IEX. However, these separation modes suffer from low separation resolution.…”
Section: Discussionmentioning
confidence: 99%
“…Similarly, here we monitored the charge-state distribution (CSD) of BSA (monomer; M) at various ionic-strength conditions of ammonium acetate, 10 and observed changes in the compactness of the protein. Lowering the salt concentration of the mobile phase caused a shift towards higher charge states and, thus, lower m/z (see Figure 1B), suggesting the presence of a less-compact protein structure 11 . This indicates that with the stationary phase adopted in this study high ionic strength (> 200 mM) are required to achieve (almost) interaction-free SEC and protect the protein structure from possible denaturation or unfolding.…”
Section: Monitoring Native Structures With Micro Flow Sec-nms -Effect...mentioning
confidence: 99%
“…As an alternative to laborious samplepreparation processes, comprehensive characterization of biotherapeutic proteins and biological samples typically involves efficient analytical separations (e.g. SEC, ion-exchange chromatography, IEX, hydrophobicinteraction chromatography, HIC) prior to detection by nMS 11 .…”
Section: Introductionmentioning
confidence: 99%