Combination of High-Resolution Multistage Ion Mobility and Tandem MS with High Energy of Activation to Resolve the Structure of Complex Chemoenzymatically Synthesized Glycans
Carbohydrates, in particular microbial glycans, are highly structurally diverse biomolecules, the recognition of which governs numerous biological processes. Of special interest, glycans of known monosaccharide composition feature multiple possible isomers, differentiated by the anomerism and positi...
Saved in:
Published in | Analytical chemistry (Washington) Vol. 94; no. 4; pp. 2279 - 2287 |
---|---|
Main Authors | , , , , , , , , |
Format | Journal Article |
Language | English |
Published |
United States
American Chemical Society
01.02.2022
|
Subjects | |
Online Access | Get full text |
Cover
Loading…
Abstract | Carbohydrates, in particular microbial glycans, are highly structurally diverse biomolecules, the recognition of which governs numerous biological processes. Of special interest, glycans of known monosaccharide composition feature multiple possible isomers, differentiated by the anomerism and position of their glycosidic linkages. Robust analytical tools able to circumvent this extreme structural complexity are increasing in demand to ensure not only the correct determination of naturally occurring glycans but also to support the rapid development of enzymatic and chemoenzymatic glycan synthesis. In support to the later, we report the use of complementary strategies based on mass spectrometry (MS) to evaluate the ability of 14 engineered mutants of sucrose-utilizing α-transglucosylases to produce type/group-specific Shigella flexneri pentasaccharide bricks from a single lightly protected non-natural tetrasaccharide acceptor substrate. A first analysis of the reaction media by UHPLC coupled to high-accuracy MS led to detect six reaction products of enzymatic glucosylation out of the eight possible ones. A seventh structure was evidenced by an additional step of ion mobility at a resolving power (R p) of approximately 100. Finally, a R p of about 250 in ion mobility made it possible to detect the eighth and last of the expected structures. Complementary to these measurements, tandem MS with high activation energy charge transfer dissociation (CTD) allowed us to unambiguously characterize seven regioisomers out of the eight possible products of enzymatic glucosylation. This work illustrates the potential of the recently described powerful IMS and CTD–MS methods for the precise structural characterization of complex glycans. |
---|---|
AbstractList | Carbohydrates, in particular microbial glycans, are highly structurally diverse biomolecules, the recognition of which governs numerous biological processes. Of special interest, glycans of known monosaccharide composition feature multiple possible isomers, differentiated by the anomerism and position of their glycosidic linkages. Robust analytical tools able to circumvent this extreme structural complexity are increasing in demand to ensure not only the correct determination of naturally occurring glycans but also to support the rapid development of enzymatic and chemoenzymatic glycan synthesis. In support to the later, we report the use of complementary strategies based on mass spectrometry (MS) to evaluate the ability of 14 engineered mutants of sucrose-utilizing α-transglucosylases to produce type/group-specific Shigella flexneri pentasaccharide bricks from a single lightly protected non-natural tetrasaccharide acceptor substrate. A first analysis of the reaction media by UHPLC coupled to high-accuracy MS led to detect six reaction products of enzymatic glucosylation out of the eight possible ones. A seventh structure was evidenced by an additional step of ion mobility at a resolving power (Rp) of approximately 100. Finally, a Rp of about 250 in ion mobility made it possible to detect the eighth and last of the expected structures. Complementary to these measurements, tandem MS with high activation energy charge transfer dissociation (CTD) allowed us to unambiguously characterize seven regioisomers out of the eight possible products of enzymatic glucosylation. This work illustrates the potential of the recently described powerful IMS and CTD–MS methods for the precise structural characterization of complex glycans. Carbohydrates, in particular microbial glycans, are highly structurally diverse biomolecules, the recognition of which governs numerousbiological processes. Of special interest, glycans of known monosaccharide composition feature multiple possible isomers, differentiated by the anomerism and position of their glycosidic linkages. Robust analytical tools able to circumvent this extreme structural complexity are increasing in demand to ensure not only the correct determination of naturally occurring glycans but also to support the rapid development of enzymatic and chemoenzymatic glycan synthesis. In support to the later, we report the use of complementary strategies based on mass spectrometry (MS) to evaluate the ability of 14 engineered mutants of sucrose-utilizing α-transglucosylases to produce type/group-specific Shigella flexneri pentasaccharide bricks from a single lightly protected non-natural tetrasaccharide acceptor substrate. A first analysis of the reaction media by UHPLC coupled to high-accuracy MS led to detect six reaction products of enzymatic glucosylation out of the eight possible ones. A seventh structure was evidenced by an additional step of ion mobility at a resolving power (Rp) of approximately 100. Finally, a Rp of about 250 in ion mobility made it possible to detect the eighth and last of the expected structures. Complementary to these measurements, tandem MS with high activation energy charge transfer dissociation (CTD) allowed us to unambiguously characterize seven regioisomers out of the eight possible products of enzymatic glucosylation. This work illustrates the potential of the recently described powerful IMS and CTD−MS methods for the precise structural characterization of complex glycans. Carbohydrates, in particular microbial glycans, are highly structurally diverse biomolecules, the recognition of which governs numerous biological processes. Of special interest, glycans of known monosaccharide composition feature multiple possible isomers, differentiated by the anomerism and position of their glycosidic linkages. Robust analytical tools able to circumvent this extreme structural complexity are increasing in demand to ensure not only the correct determination of naturally occurring glycans but also to support the rapid development of enzymatic and chemoenzymatic glycan synthesis. In support to the later, we report the use of complementary strategies based on mass spectrometry (MS) to evaluate the ability of 14 engineered mutants of sucrose-utilizing α-transglucosylases to produce type/group-specific Shigella flexneri pentasaccharide bricks from a single lightly protected non-natural tetrasaccharide acceptor substrate. A first analysis of the reaction media by UHPLC coupled to high-accuracy MS led to detect six reaction products of enzymatic glucosylation out of the eight possible ones. A seventh structure was evidenced by an additional step of ion mobility at a resolving power (Rₚ) of approximately 100. Finally, a Rₚ of about 250 in ion mobility made it possible to detect the eighth and last of the expected structures. Complementary to these measurements, tandem MS with high activation energy charge transfer dissociation (CTD) allowed us to unambiguously characterize seven regioisomers out of the eight possible products of enzymatic glucosylation. This work illustrates the potential of the recently described powerful IMS and CTD–MS methods for the precise structural characterization of complex glycans. Carbohydrates, in particular microbial glycans, are highly structurally diverse biomolecules, the recognition of which governs numerous biological processes. Of special interest, glycans of known monosaccharide composition feature multiple possible isomers, differentiated by the anomerism and position of their glycosidic linkages. Robust analytical tools able to circumvent this extreme structural complexity are increasing in demand to ensure not only the correct determination of naturally occurring glycans but also to support the rapid development of enzymatic and chemoenzymatic glycan synthesis. In support to the later, we report the use of complementary strategies based on mass spectrometry (MS) to evaluate the ability of 14 engineered mutants of sucrose-utilizing α-transglucosylases to produce type/group-specific Shigella flexneri pentasaccharide bricks from a single lightly protected non-natural tetrasaccharide acceptor substrate. A first analysis of the reaction media by UHPLC coupled to high-accuracy MS led to detect six reaction products of enzymatic glucosylation out of the eight possible ones. A seventh structure was evidenced by an additional step of ion mobility at a resolving power (Rp) of approximately 100. Finally, a Rp of about 250 in ion mobility made it possible to detect the eighth and last of the expected structures. Complementary to these measurements, tandem MS with high activation energy charge transfer dissociation (CTD) allowed us to unambiguously characterize seven regioisomers out of the eight possible products of enzymatic glucosylation. This work illustrates the potential of the recently described powerful IMS and CTD-MS methods for the precise structural characterization of complex glycans.Carbohydrates, in particular microbial glycans, are highly structurally diverse biomolecules, the recognition of which governs numerous biological processes. Of special interest, glycans of known monosaccharide composition feature multiple possible isomers, differentiated by the anomerism and position of their glycosidic linkages. Robust analytical tools able to circumvent this extreme structural complexity are increasing in demand to ensure not only the correct determination of naturally occurring glycans but also to support the rapid development of enzymatic and chemoenzymatic glycan synthesis. In support to the later, we report the use of complementary strategies based on mass spectrometry (MS) to evaluate the ability of 14 engineered mutants of sucrose-utilizing α-transglucosylases to produce type/group-specific Shigella flexneri pentasaccharide bricks from a single lightly protected non-natural tetrasaccharide acceptor substrate. A first analysis of the reaction media by UHPLC coupled to high-accuracy MS led to detect six reaction products of enzymatic glucosylation out of the eight possible ones. A seventh structure was evidenced by an additional step of ion mobility at a resolving power (Rp) of approximately 100. Finally, a Rp of about 250 in ion mobility made it possible to detect the eighth and last of the expected structures. Complementary to these measurements, tandem MS with high activation energy charge transfer dissociation (CTD) allowed us to unambiguously characterize seven regioisomers out of the eight possible products of enzymatic glucosylation. This work illustrates the potential of the recently described powerful IMS and CTD-MS methods for the precise structural characterization of complex glycans. Carbohydrates, in particular microbial glycans, are highly structurally diverse biomolecules, the recognition of which governs numerous biological processes. Of special interest, glycans of known monosaccharide composition feature multiple possible isomers, differentiated by the anomerism and position of their glycosidic linkages. Robust analytical tools able to circumvent this extreme structural complexity are increasing in demand to ensure not only the correct determination of naturally occurring glycans but also to support the rapid development of enzymatic and chemoenzymatic glycan synthesis. In support to the later, we report the use of complementary strategies based on mass spectrometry (MS) to evaluate the ability of 14 engineered mutants of sucrose-utilizing α-transglucosylases to produce type/group-specific pentasaccharide bricks from a single lightly protected non-natural tetrasaccharide acceptor substrate. A first analysis of the reaction media by UHPLC coupled to high-accuracy MS led to detect six reaction products of enzymatic glucosylation out of the eight possible ones. A seventh structure was evidenced by an additional step of ion mobility at a resolving power ( ) of approximately 100. Finally, a of about 250 in ion mobility made it possible to detect the eighth and last of the expected structures. Complementary to these measurements, tandem MS with high activation energy charge transfer dissociation (CTD) allowed us to unambiguously characterize seven regioisomers out of the eight possible products of enzymatic glucosylation. This work illustrates the potential of the recently described powerful IMS and CTD-MS methods for the precise structural characterization of complex glycans. Carbohydrates, in particular microbial glycans, are highly structurally diverse biomolecules, the recognition of which governs numerous biological processes. Of special interest, glycans of known monosaccharide composition feature multiple possible isomers, differentiated by the anomerism and position of their glycosidic linkages. Robust analytical tools able to circumvent this extreme structural complexity are increasing in demand to ensure not only the correct determination of naturally occurring glycans but also to support the rapid development of enzymatic and chemoenzymatic glycan synthesis. In support to the later, we report the use of complementary strategies based on mass spectrometry (MS) to evaluate the ability of 14 engineered mutants of sucrose-utilizing α-transglucosylases to produce type/group-specific Shigella flexneri pentasaccharide bricks from a single lightly protected non-natural tetrasaccharide acceptor substrate. A first analysis of the reaction media by UHPLC coupled to high-accuracy MS led to detect six reaction products of enzymatic glucosylation out of the eight possible ones. A seventh structure was evidenced by an additional step of ion mobility at a resolving power (R p) of approximately 100. Finally, a R p of about 250 in ion mobility made it possible to detect the eighth and last of the expected structures. Complementary to these measurements, tandem MS with high activation energy charge transfer dissociation (CTD) allowed us to unambiguously characterize seven regioisomers out of the eight possible products of enzymatic glucosylation. This work illustrates the potential of the recently described powerful IMS and CTD–MS methods for the precise structural characterization of complex glycans. |
Author | Lissarrague, Adrien Rogniaux, Hélène Ollivier, Simon Mulard, Laurence A Guieysse, David Fanuel, Mathieu André, Isabelle Ropartz, David Benkoulouche, Mounir |
AuthorAffiliation | INRAE, UR BIA Institut Pasteur, Université de Paris, CNRS UMR3523, Unité de Chimie des Biomolécules INRAE, BIBS Facility Toulouse Biotechnology Institute, TBI, Université de Toulouse, CNRS, INRAE, INSA |
AuthorAffiliation_xml | – name: INRAE, UR BIA – name: INRAE, BIBS Facility – name: Toulouse Biotechnology Institute, TBI, Université de Toulouse, CNRS, INRAE, INSA – name: Institut Pasteur, Université de Paris, CNRS UMR3523, Unité de Chimie des Biomolécules |
Author_xml | – sequence: 1 givenname: David orcidid: 0000-0003-4767-6940 surname: Ropartz fullname: Ropartz, David organization: INRAE, BIBS Facility – sequence: 2 givenname: Mathieu orcidid: 0000-0001-8384-8266 surname: Fanuel fullname: Fanuel, Mathieu organization: INRAE, BIBS Facility – sequence: 3 givenname: Simon orcidid: 0000-0002-7671-1736 surname: Ollivier fullname: Ollivier, Simon organization: INRAE, BIBS Facility – sequence: 4 givenname: Adrien surname: Lissarrague fullname: Lissarrague, Adrien organization: INRAE, BIBS Facility – sequence: 5 givenname: Mounir surname: Benkoulouche fullname: Benkoulouche, Mounir organization: Toulouse Biotechnology Institute, TBI, Université de Toulouse, CNRS, INRAE, INSA – sequence: 6 givenname: Laurence A orcidid: 0000-0002-5622-1422 surname: Mulard fullname: Mulard, Laurence A organization: Institut Pasteur, Université de Paris, CNRS UMR3523, Unité de Chimie des Biomolécules – sequence: 7 givenname: Isabelle orcidid: 0000-0001-6280-4109 surname: André fullname: André, Isabelle organization: Toulouse Biotechnology Institute, TBI, Université de Toulouse, CNRS, INRAE, INSA – sequence: 8 givenname: David surname: Guieysse fullname: Guieysse, David organization: Toulouse Biotechnology Institute, TBI, Université de Toulouse, CNRS, INRAE, INSA – sequence: 9 givenname: Hélène orcidid: 0000-0001-6083-2034 surname: Rogniaux fullname: Rogniaux, Hélène email: helene.rogniaux@inrae.fr organization: INRAE, BIBS Facility |
BackLink | https://www.ncbi.nlm.nih.gov/pubmed/35049286$$D View this record in MEDLINE/PubMed https://hal.inrae.fr/hal-03573196$$DView record in HAL |
BookMark | eNqFkt9u2yAYxdHUaU27vcE0Ie1mvXAG_oNhd1HUNZVSTVq6a0QwJFTYZAZncx-qzzgcJ73oxSokEB-_cwB95wKcNa5RAHzEaIpRir8K6aeiEVZuVT3FEuWMpm_ABBcpSgil6RmYIISyJC0ROgcX3j8ghDHC5B04z4qIp5RMwNPc1WvTiGBcA52GC7PZJj-Vd7Y7lO46G4wPYqPg7bB1a2NN6KFoKngfJ1XDuxX8Y8L2IIXXjWo3_eA0k8HsR9_g4MFyr2DYKrgKbSdD16oBi_fvrPoL5_EbTjWPfR01Uljbw1XfRNybR1XBG9tL0fj34K0W1qsPx_US_Pp-fT9fJMsfN7fz2TIROWUhISXJVSVIKbKqyJRCVJdE54RVeaUlWbNUUqWJWBNZac2KkgmtsSaUIULjyC7B1ei7FZbvWlOLtudOGL6YLflQQ1lRZpiRPY7sl5Hdte53p3zgtfFSWSsa5TrPU5JTWrDR9jU0xYTggrKIfn6BPriujf0-UCRlFBU0Up-OVLeuVfX81FODI_BtBGTrvG-V5tKEQ1dCK4zlGPEhTTymiZ_SxI9piuL8hfjk_4oMjbLh9PnV_5X8A7gS5KU |
CitedBy_id | crossref_primary_10_1016_j_cbpa_2023_102424 crossref_primary_10_1016_j_trac_2024_117721 crossref_primary_10_1002_rcm_9750 crossref_primary_10_1016_j_foodchem_2025_143839 crossref_primary_10_1146_annurev_anchem_091522_031329 crossref_primary_10_1021_jasms_2c00333 crossref_primary_10_1016_j_trac_2022_116761 |
Cites_doi | 10.1080/21645515.2019.1606972 10.1038/s41598-021-99384-9 10.1007/s13361-014-0989-6 10.1093/bioinformatics/btn323 10.1021/acs.chemrev.1c00260 10.1021/acs.analchem.0c03173 10.1021/acs.analchem.9b01838 10.1038/s41581-019-0129-4 10.1371/journal.pone.0044913 10.1039/d0ra04471g 10.1021/acs.analchem.9b03036 10.1002/jssc.202000878 10.3390/microorganisms9071382 10.1093/glycob/cww086 10.1038/s41579-018-0007-2 10.1021/ac502054p 10.1021/acs.analchem.7b00185 10.1039/c8cc06966b 10.1021/acs.joc.0c00777 10.1126/scitranslmed.aat4615 10.1007/s13361-016-1453-6 10.1002/cbic.202100327 10.1021/acs.analchem.1c01244 10.1021/acs.analchem.7b00473 10.1016/s1473-3099(20)30488-6 10.1021/acs.bioconjchem.5b00617 10.1021/jasms.0c00252 10.1002/mas.21563 10.1016/s1473-3099(18)30475-4 10.1007/s13361-019-02168-9 10.3389/fcimb.2019.00117 10.1021/acs.analchem.9b02808 10.1134/s0006297915070093 10.1093/glycob/4.6.759 10.1002/rcm.1641 10.1039/d1an00780g 10.1021/jasms.0c00087 10.1021/acs.analchem.1c00673 10.1021/acs.chemrev.9b00440 10.1038/s41598-021-81719-1 10.1042/bst20190788 10.1111/febs.15909 10.1111/j.1574-695x.2012.01000.x |
ContentType | Journal Article |
Copyright | 2022 American Chemical Society Copyright American Chemical Society Feb 1, 2022 Distributed under a Creative Commons Attribution 4.0 International License |
Copyright_xml | – notice: 2022 American Chemical Society – notice: Copyright American Chemical Society Feb 1, 2022 – notice: Distributed under a Creative Commons Attribution 4.0 International License |
DBID | AAYXX CITATION CGR CUY CVF ECM EIF NPM 7QF 7QO 7QQ 7SC 7SE 7SP 7SR 7TA 7TB 7TM 7U5 7U7 7U9 8BQ 8FD C1K F28 FR3 H8D H8G H94 JG9 JQ2 KR7 L7M L~C L~D P64 7X8 7S9 L.6 1XC VOOES |
DOI | 10.1021/acs.analchem.1c04982 |
DatabaseName | CrossRef Medline MEDLINE MEDLINE (Ovid) MEDLINE MEDLINE PubMed Aluminium Industry Abstracts Biotechnology Research Abstracts Ceramic Abstracts Computer and Information Systems Abstracts Corrosion Abstracts Electronics & Communications Abstracts Engineered Materials Abstracts Materials Business File Mechanical & Transportation Engineering Abstracts Nucleic Acids Abstracts Solid State and Superconductivity Abstracts Toxicology Abstracts Virology and AIDS Abstracts METADEX Technology Research Database Environmental Sciences and Pollution Management ANTE: Abstracts in New Technology & Engineering Engineering Research Database Aerospace Database Copper Technical Reference Library AIDS and Cancer Research Abstracts Materials Research Database ProQuest Computer Science Collection Civil Engineering Abstracts Advanced Technologies Database with Aerospace Computer and Information Systems Abstracts Academic Computer and Information Systems Abstracts Professional Biotechnology and BioEngineering Abstracts MEDLINE - Academic AGRICOLA AGRICOLA - Academic Hyper Article en Ligne (HAL) Hyper Article en Ligne (HAL) (Open Access) |
DatabaseTitle | CrossRef MEDLINE Medline Complete MEDLINE with Full Text PubMed MEDLINE (Ovid) Materials Research Database Technology Research Database Computer and Information Systems Abstracts – Academic Mechanical & Transportation Engineering Abstracts Nucleic Acids Abstracts ProQuest Computer Science Collection Computer and Information Systems Abstracts Materials Business File Environmental Sciences and Pollution Management Aerospace Database Copper Technical Reference Library Engineered Materials Abstracts Biotechnology Research Abstracts AIDS and Cancer Research Abstracts Advanced Technologies Database with Aerospace ANTE: Abstracts in New Technology & Engineering Civil Engineering Abstracts Aluminium Industry Abstracts Virology and AIDS Abstracts Toxicology Abstracts Electronics & Communications Abstracts Ceramic Abstracts METADEX Biotechnology and BioEngineering Abstracts Computer and Information Systems Abstracts Professional Solid State and Superconductivity Abstracts Engineering Research Database Corrosion Abstracts MEDLINE - Academic AGRICOLA AGRICOLA - Academic |
DatabaseTitleList | Materials Research Database AGRICOLA MEDLINE - Academic MEDLINE |
Database_xml | – sequence: 1 dbid: NPM name: PubMed url: https://proxy.k.utb.cz/login?url=http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?db=PubMed sourceTypes: Index Database – sequence: 2 dbid: EIF name: MEDLINE url: https://proxy.k.utb.cz/login?url=https://www.webofscience.com/wos/medline/basic-search sourceTypes: Index Database |
DeliveryMethod | fulltext_linktorsrc |
Discipline | Engineering Chemistry |
EISSN | 1520-6882 |
EndPage | 2287 |
ExternalDocumentID | oai_HAL_hal_03573196v1 35049286 10_1021_acs_analchem_1c04982 a358157684 |
Genre | Research Support, Non-U.S. Gov't Journal Article |
GroupedDBID | - 02 23M 4.4 55A 5GY 5RE 5VS 7~N 85S AABXI ABFLS ABFRP ABMVS ABOCM ABPPZ ABPTK ABUCX ACGFS ACGOD ACIWK ACJ ACNCT ACPRK ACS AEESW AENEX AFEFF AFRAH AGXLV AHGAQ ALMA_UNASSIGNED_HOLDINGS AQSVZ BAANH BKOMP CS3 D0L DZ EBS ED F5P GGK GNL IH9 IHE JG K2 P2P PQEST PQQKQ ROL RXW TAE TN5 UHB UI2 UKR VF5 VG9 VQA W1F WH7 X X6Y XOL YZZ --- -DZ -~X .DC .K2 53G 6J9 AAHBH AAYXX ABBLG ABHFT ABHMW ABJNI ABLBI ABQRX ACBEA ACGFO ACKOT ADHLV CITATION CUPRZ ED~ JG~ KZ1 LMP XSW ZCA ~02 CGR CUY CVF ECM EIF NPM YIN 7QF 7QO 7QQ 7SC 7SE 7SP 7SR 7TA 7TB 7TM 7U5 7U7 7U9 8BQ 8FD C1K F28 FR3 H8D H8G H94 JG9 JQ2 KR7 L7M L~C L~D P64 7X8 7S9 L.6 1XC UMC VOOES |
ID | FETCH-LOGICAL-a489t-6764eda67a3d53ee08f76f469d4dfc6b92c8ef6ab6cdff9579aff1f6890686863 |
IEDL.DBID | ACS |
ISSN | 0003-2700 1520-6882 |
IngestDate | Fri May 09 12:16:19 EDT 2025 Fri Jul 11 12:35:34 EDT 2025 Fri Jul 11 16:56:21 EDT 2025 Mon Jun 30 08:42:45 EDT 2025 Wed Feb 19 02:27:12 EST 2025 Tue Jul 01 01:19:38 EDT 2025 Thu Apr 24 23:03:52 EDT 2025 Thu Feb 03 05:58:50 EST 2022 |
IsDoiOpenAccess | true |
IsOpenAccess | true |
IsPeerReviewed | true |
IsScholarly | true |
Issue | 4 |
Language | English |
License | https://doi.org/10.15223/policy-029 https://doi.org/10.15223/policy-037 https://doi.org/10.15223/policy-045 Distributed under a Creative Commons Attribution 4.0 International License: http://creativecommons.org/licenses/by/4.0 |
LinkModel | DirectLink |
MergedId | FETCHMERGED-LOGICAL-a489t-6764eda67a3d53ee08f76f469d4dfc6b92c8ef6ab6cdff9579aff1f6890686863 |
Notes | ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 14 content type line 23 |
ORCID | 0000-0003-4767-6940 0000-0002-5622-1422 0000-0002-7671-1736 0000-0001-6083-2034 0000-0001-6280-4109 0000-0001-8384-8266 |
OpenAccessLink | https://hal.inrae.fr/hal-03573196 |
PMID | 35049286 |
PQID | 2626298058 |
PQPubID | 45400 |
PageCount | 9 |
ParticipantIDs | hal_primary_oai_HAL_hal_03573196v1 proquest_miscellaneous_2648859686 proquest_miscellaneous_2621661589 proquest_journals_2626298058 pubmed_primary_35049286 crossref_citationtrail_10_1021_acs_analchem_1c04982 crossref_primary_10_1021_acs_analchem_1c04982 acs_journals_10_1021_acs_analchem_1c04982 |
ProviderPackageCode | CITATION AAYXX |
PublicationCentury | 2000 |
PublicationDate | 2022-02-01 |
PublicationDateYYYYMMDD | 2022-02-01 |
PublicationDate_xml | – month: 02 year: 2022 text: 2022-02-01 day: 01 |
PublicationDecade | 2020 |
PublicationPlace | United States |
PublicationPlace_xml | – name: United States – name: Washington |
PublicationTitle | Analytical chemistry (Washington) |
PublicationTitleAlternate | Anal. Chem |
PublicationYear | 2022 |
Publisher | American Chemical Society |
Publisher_xml | – name: American Chemical Society |
References | ref9/cit9 ref6/cit6 ref36/cit36 ref3/cit3 ref27/cit27 ref18/cit18 ref11/cit11 ref25/cit25 ref16/cit16 ref29/cit29 ref32/cit32 ref23/cit23 ref39/cit39 ref14/cit14 ref8/cit8 Giles K. (ref19/cit19) 2014 ref5/cit5 ref31/cit31 ref2/cit2 ref43/cit43 ref34/cit34 ref37/cit37 ref28/cit28 ref40/cit40 ref20/cit20 ref17/cit17 ref10/cit10 ref26/cit26 ref35/cit35 ref21/cit21 ref12/cit12 ref15/cit15 ref42/cit42 ref41/cit41 ref22/cit22 ref13/cit13 ref33/cit33 ref4/cit4 ref30/cit30 ref1/cit1 ref24/cit24 ref38/cit38 ref44/cit44 ref7/cit7 |
References_xml | – ident: ref9/cit9 doi: 10.1080/21645515.2019.1606972 – ident: ref34/cit34 doi: 10.1038/s41598-021-99384-9 – ident: ref39/cit39 doi: 10.1007/s13361-014-0989-6 – ident: ref40/cit40 doi: 10.1093/bioinformatics/btn323 – ident: ref44/cit44 doi: 10.1021/acs.chemrev.1c00260 – ident: ref26/cit26 doi: 10.1021/acs.analchem.0c03173 – ident: ref20/cit20 doi: 10.1021/acs.analchem.9b01838 – ident: ref4/cit4 doi: 10.1038/s41581-019-0129-4 – ident: ref41/cit41 doi: 10.1371/journal.pone.0044913 – ident: ref7/cit7 doi: 10.1039/d0ra04471g – ident: ref23/cit23 doi: 10.1021/acs.analchem.9b03036 – ident: ref13/cit13 doi: 10.1002/jssc.202000878 – ident: ref37/cit37 doi: 10.3390/microorganisms9071382 – ident: ref3/cit3 doi: 10.1093/glycob/cww086 – ident: ref5/cit5 doi: 10.1038/s41579-018-0007-2 – ident: ref15/cit15 doi: 10.1021/ac502054p – ident: ref17/cit17 doi: 10.1021/acs.analchem.7b00185 – ident: ref18/cit18 doi: 10.1039/c8cc06966b – ident: ref38/cit38 doi: 10.1021/acs.joc.0c00777 – ident: ref8/cit8 doi: 10.1126/scitranslmed.aat4615 – ident: ref30/cit30 doi: 10.1007/s13361-016-1453-6 – ident: ref2/cit2 doi: 10.1002/cbic.202100327 – ident: ref25/cit25 doi: 10.1021/acs.analchem.1c01244 – ident: ref31/cit31 doi: 10.1021/acs.analchem.7b00473 – ident: ref12/cit12 doi: 10.1016/s1473-3099(20)30488-6 – ident: ref11/cit11 doi: 10.1021/acs.bioconjchem.5b00617 – ident: ref33/cit33 doi: 10.1021/jasms.0c00252 – ident: ref28/cit28 doi: 10.1002/mas.21563 – ident: ref36/cit36 doi: 10.1016/s1473-3099(18)30475-4 – ident: ref22/cit22 doi: 10.1007/s13361-019-02168-9 – ident: ref6/cit6 doi: 10.3389/fcimb.2019.00117 – ident: ref16/cit16 doi: 10.1021/acs.analchem.9b02808 – ident: ref43/cit43 doi: 10.1134/s0006297915070093 – ident: ref1/cit1 doi: 10.1093/glycob/4.6.759 – ident: ref14/cit14 doi: 10.1002/rcm.1641 – ident: ref27/cit27 doi: 10.1039/d1an00780g – volume-title: In Annual Conference Proceedings year: 2014 ident: ref19/cit19 – ident: ref32/cit32 doi: 10.1021/jasms.0c00087 – ident: ref24/cit24 doi: 10.1021/acs.analchem.1c00673 – ident: ref29/cit29 doi: 10.1021/acs.chemrev.9b00440 – ident: ref35/cit35 doi: 10.1038/s41598-021-81719-1 – ident: ref21/cit21 doi: 10.1042/bst20190788 – ident: ref10/cit10 doi: 10.1111/febs.15909 – ident: ref42/cit42 doi: 10.1111/j.1574-695x.2012.01000.x |
SSID | ssj0011016 |
Score | 2.43095 |
Snippet | Carbohydrates, in particular microbial glycans, are highly structurally diverse biomolecules, the recognition of which governs numerous biological processes.... Carbohydrates, in particular microbial glycans, are highly structurally diverse biomolecules, the recognition of which governs numerousbiological processes. Of... |
SourceID | hal proquest pubmed crossref acs |
SourceType | Open Access Repository Aggregation Database Index Database Enrichment Source Publisher |
StartPage | 2279 |
SubjectTerms | Activation energy analytical chemistry Biochemistry, Molecular Biology Biological activity Biomolecules Carbohydrates Charge transfer Chemistry Complexity dissociation energy Energy charge Energy of dissociation Food engineering glucosylation Glycan Ionic mobility Isomerism Isomers Life Sciences Mass spectrometry Mass spectroscopy Microorganisms Mobility Monosaccharides Oligosaccharides - chemistry Polysaccharides Polysaccharides - chemistry positional isomers Reaction products Resolution Shigella flexneri Structural analysis Substrates Sucrose Tandem Mass Spectrometry |
Title | Combination of High-Resolution Multistage Ion Mobility and Tandem MS with High Energy of Activation to Resolve the Structure of Complex Chemoenzymatically Synthesized Glycans |
URI | http://dx.doi.org/10.1021/acs.analchem.1c04982 https://www.ncbi.nlm.nih.gov/pubmed/35049286 https://www.proquest.com/docview/2626298058 https://www.proquest.com/docview/2621661589 https://www.proquest.com/docview/2648859686 https://hal.inrae.fr/hal-03573196 |
Volume | 94 |
hasFullText | 1 |
inHoldings | 1 |
isFullTextHit | |
isPrint | |
link | http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwlV1Lb9QwELagHKAHHoWWQEEGceGQJYkTxzmuVm0XROGwrdRb5PhBEWmCyG5F9kfxG5lxHi2gUjhudmw59ufJZ8-LkFeAEaBs6NQutPTjVDC_ANrsiyQwSgibGlcz8vADnx_H706Sk4uD4u8W_Ch8I1UzkTCp8A5nk1ABoxWgcm9FHPYxUqHZYrQa4El0qJCHBtUhVO6KXvCDpJpfPkg3T9Ed8iqu6b45-_fIxyFyp3M1-TJZLYuJWv-ZyPEfX-c-udvTTzrt8PKA3DDVFrk9G6q-bZHNSwkKH5IfoC7g6OxWj9aWoleIjzf-HV6pC98FfvnJ0Lf4s3auti2VlaZHeD19Rg8XFO96XVO65yINsaepGuqq0WVNXZfnhgIbpQuX0Xb1zaAYqqvSfKc4wtpU69ZlmJVl2dJFW4F483ltND0oW4BI84gc7-8dzeZ-X-HBl7HIlj5PeWy05KlkOmHGBAAObuHErmNtFS-ySAljuSy40taiRVFaG1ouMoxsEZxtk42qrsxjQnWsuFWaRVZajNQWATDTMAIdxkJoyTzyGqY-73dokzvjexTm-HBYj7xfD4-wARK56lOlY8WO8ppW_tjqa5cq5Br5l4C2URTzfM-n73N8FrAkRd14HnpkdwDjxdgjOIXCBgsS4ZEX498AFDT2yMrUKycTAvdKRPY3GVDfSQYT6ZGdDujjcFgCg4wEf_If8_aU3IkwOsQ5te-SDcCLeQacbVk8dxv1J5oVPs4 |
linkProvider | American Chemical Society |
linkToHtml | http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwlV1Lc9MwENaUcigceJSXoYBguHBwsC1blo-ZTEsKSS9Jmd48ih7QqWszOOng_Ch-I7uK7QIzpdNjlJVmLX1arbQvQt4BRkBlQ6d2oaUfp4L5C1CbfZEERglhU-NqRk6P-Pg4_nSSnGyRpIuFASZqGKl2RvzL7ALhB2yTMLfwKeeDUIFiK0Dy3gZ9JEJgD0ez3niAF9KuUB7aVbuIuStGwXNJ1X-dS7e-oVfkVSqnO3oO7pMvPdPO4-RssFouBmr9Tz7HG3_VA3KvVUbpcIOeh2TLlLtkZ9TVgNsld_9IV_iI_ALhARdpt5a0shR9RHx8_9-gl7pgXtA2vxp6iD8r53jbUFlqOsfH6nM6nVF8-XVd6b6LO8SRhqqrskaXFXVDXhgKuimdufy2qx8GyVB4FeYnRQ4rU64bl29WFkVDZ00J5PXp2mj6sWgAMPVjcnywPx-N_bbegy9jkS19nvLYaMlTyXTCjAkAKtzC_V3H2iq-yCIljOVywZW2Fu2L0trQcpFhnIvg7AnZLqvSPCNUx4pbpVlkpcW4bRGAnhpGINFYCD2ZR97D1Oftfq1zZ4qPwhwbu_XI2_XwCOuQkas2cTrW7yiu6eX3vb5vEodcQ_8WQNeTYtbv8XCSY1vAkhQl5UXokb0Ok5e8R3Anhe0WJMIjb_q_ASho-pGlqVaOJgRNLBHZ_2hAmCcZTKRHnm7w3rPDEmAyEvz5DebtNdkZz6eTfHJ49PkFuRNh3Ihzd98j24Ad8xK0ueXildu7vwFLpkcv |
linkToPdf | http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwnV1Lb9QwELagSDwOPMorUMAgLhyyJHHiOMfV0mULbYW0rVRxiRw_AJEmFdmtyP4ofiMz3iQUpFLBMc7Ymtifx-PMi5CXgBFQ2dCpXWjpx6lgfgFqsy-SwCghbGpczci9fT47jN8dJUdnSn0BEw2M1DgjPu7qE227DAPha2yXML_wOcejUIFyK0D6XkHLHYJ7PJkPBgS8lPbF8tC22kfNnTMKnk2q-e1suvwZPSPPUzvd8TO9RT4OjDuvk6-j5aIYqdUfOR3_68tuk5udUkrHaxTdIZdMtUmuTfpacJvkxpm0hXfJDxAicKF2a0prS9FXxEc7wBrF1AX1gtb5ydAdfKydA25LZaXpAf60PqZ7c4p_gF1Xuu3iD3GkseqrrdFFTd2Qp4aCjkrnLs_t8ptBMhRipflOkcPaVKvW5Z2VZdnSeVsBefNlZTR9W7YAnOYeOZxuH0xmflf3wZexyBY-T3lstOSpZDphxgQAGW7hHq9jbRUvskgJY7ksuNLWop1RWhtaLjKMdxGc3ScbVV2Zh4TqWHGrNIustBi_LQLQV8MIJBsLoSfzyCuY-rzbt03uTPJRmGNjvx55tx4eYT06ctUlUMc6HuUFvfyh18k6gcgF9C8AeAMpZv-ejXdzbAtYkqLEPA09stXj8hfvEdxNYdsFifDI8-E1AAVNQLIy9dLRhKCRJSL7Gw0I9SSDifTIgzXmB3ZYAkxGgj_6h3l7Rq5-eDPNd3f23z8m1yMMH3Fe71tkA6BjnoBStyieuu37E5XKSbI |
openUrl | ctx_ver=Z39.88-2004&ctx_enc=info%3Aofi%2Fenc%3AUTF-8&rfr_id=info%3Asid%2Fsummon.serialssolutions.com&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Ajournal&rft.genre=article&rft.atitle=Combination+of+High-Resolution+Multistage+Ion+Mobility+and+Tandem+MS+with+High+Energy+of+Activation+to+Resolve+the+Structure+of+Complex+Chemoenzymatically+Synthesized+Glycans&rft.jtitle=Analytical+chemistry+%28Washington%29&rft.au=Ropartz%2C+David&rft.au=Fanuel%2C+Mathieu&rft.au=Ollivier%2C+Simon&rft.au=Lissarrague%2C+Adrien&rft.date=2022-02-01&rft.issn=1520-6882&rft.volume=94&rft.issue=4+p.2279-2287&rft.spage=2279&rft.epage=2287&rft_id=info:doi/10.1021%2Facs.analchem.1c04982&rft.externalDBID=NO_FULL_TEXT |
thumbnail_l | http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/lc.gif&issn=0003-2700&client=summon |
thumbnail_m | http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/mc.gif&issn=0003-2700&client=summon |
thumbnail_s | http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/sc.gif&issn=0003-2700&client=summon |