Identifying Membrane Protein–Lipid Interactions with Lipidomic Lipid Exchange-Mass Spectrometry
Lipids can play important roles in modulating membrane protein structure and function. However, it is challenging to identify natural lipids bound to membrane proteins in complex bilayers. Here, we developed lipidomic lipid exchange-mass spectrometry (LX-MS) to study the lipid affinity for membrane...
Saved in:
| Published in: | Journal of the American Chemical Society Vol. 145; no. 38; pp. 20859 - 20867 |
|---|---|
| Main Authors: | , , , , , , , |
| Format: | Journal Article |
| Language: | English |
| Published: |
United States
American Chemical Society
27-09-2023
|
| Subjects: | |
| Online Access: | Get full text |
| Tags: |
Add Tag
No Tags, Be the first to tag this record!
|
| Abstract | Lipids can play important roles in modulating membrane protein structure and function. However, it is challenging to identify natural lipids bound to membrane proteins in complex bilayers. Here, we developed lipidomic lipid exchange-mass spectrometry (LX-MS) to study the lipid affinity for membrane proteins on a lipidomic scale. We first mix membrane protein nanodiscs with empty nanodiscs that have no embedded membrane proteins. After allowing lipids to passively exchange between the two populations, we separate the two types of nanodiscs and perform lipidomic analysis on each with liquid chromatography and MS. Enrichment of lipids in the membrane protein nanodiscs reveals the affinity of individual lipids for binding the target membrane protein. We apply this approach to study three membrane proteins. With the Escherichia coli ammonium transporter AmtB and aquaporin AqpZ in nanodiscs with E. coli polar lipid extracts, we detected binding of cardiolipin and phosphatidyl-glycerol lipids to the proteins. With the acetylcholine receptor in nanodiscs with brain polar lipid extracts, we discovered a complex set of lipid interactions that depended on the head group and tail composition. Overall, lipidomic LX-MS provides a detailed understanding of the lipid-binding affinity and thermodynamics for membrane proteins in complex bilayers and provides a unique perspective on the chemical environment surrounding membrane proteins. |
|---|---|
| AbstractList | Lipids can play important roles in modulating membrane protein structure and function. However, it is challenging to identify natural lipids bound to membrane proteins in complex bilayers. Here, we developed lipidomic lipid exchange-mass spectrometry (LX-MS) to study the lipid affinity for membrane proteins on a lipidomic scale. We first mix membrane protein nanodiscs with empty nanodiscs that have no embedded membrane proteins. After allowing lipids to passively exchange between the two populations, we separate the two types of nanodiscs and perform lipidomic analysis on each with liquid chromatography and MS. Enrichment of lipids in the membrane protein nanodiscs reveals the affinity of individual lipids for binding the target membrane protein. We apply this approach to study three membrane proteins. With the Escherichia coli ammonium transporter AmtB and aquaporin AqpZ in nanodiscs with E. coli polar lipid extracts, we detected binding of cardiolipin and phosphatidyl-glycerol lipids to the proteins. With the acetylcholine receptor in nanodiscs with brain polar lipid extracts, we discovered a complex set of lipid interactions that depended on the head group and tail composition. Overall, lipidomic LX-MS provides a detailed understanding of the lipid-binding affinity and thermodynamics for membrane proteins in complex bilayers and provides a unique perspective on the chemical environment surrounding membrane proteins.Lipids can play important roles in modulating membrane protein structure and function. However, it is challenging to identify natural lipids bound to membrane proteins in complex bilayers. Here, we developed lipidomic lipid exchange-mass spectrometry (LX-MS) to study the lipid affinity for membrane proteins on a lipidomic scale. We first mix membrane protein nanodiscs with empty nanodiscs that have no embedded membrane proteins. After allowing lipids to passively exchange between the two populations, we separate the two types of nanodiscs and perform lipidomic analysis on each with liquid chromatography and MS. Enrichment of lipids in the membrane protein nanodiscs reveals the affinity of individual lipids for binding the target membrane protein. We apply this approach to study three membrane proteins. With the Escherichia coli ammonium transporter AmtB and aquaporin AqpZ in nanodiscs with E. coli polar lipid extracts, we detected binding of cardiolipin and phosphatidyl-glycerol lipids to the proteins. With the acetylcholine receptor in nanodiscs with brain polar lipid extracts, we discovered a complex set of lipid interactions that depended on the head group and tail composition. Overall, lipidomic LX-MS provides a detailed understanding of the lipid-binding affinity and thermodynamics for membrane proteins in complex bilayers and provides a unique perspective on the chemical environment surrounding membrane proteins. Lipids can play important roles in modulating membrane protein structure and function. However, it is challenging to identify natural lipids bound to membrane proteins in complex bilayers. Here, we developed lipidomic lipid exchange-mass spectrometry (LX-MS) to study the lipid affinity for membrane proteins on a lipidomic scale. We first mix membrane protein nanodiscs with empty nanodiscs that have no embedded membrane proteins. After allowing lipids to passively exchange between the two populations, we separate the two types of nanodiscs and perform lipidomic analysis on each with liquid chromatography and mass spectrometry. Enrichment of lipids in the membrane protein nanodiscs reveals the affinity of individual lipids for binding the target membrane protein. We apply this approach to study three membrane proteins. With the E. coli ammonium transporter AmtB and aquaporin AqpZ in nanodiscs with E. coli polar lipid extract, we detected binding of cardiolipin and phosphatidyl-glycerol lipids to the proteins. With the acetylcholine receptor in nanodiscs with brain polar lipid extract, we discovered a complex set of lipid interactions that depended on the head group and tail composition. Overall, lipidomic LX-MS provides a detailed understanding of the lipid binding affinity and thermodynamics for membrane proteins in complex bilayers and provides a unique perspective on the chemical environment surrounding membrane proteins. Lipids can play important roles in modulating membrane protein structure and function. However, it is challenging to identify natural lipids bound to membrane proteins in complex bilayers. Here, we developed lipidomic lipid exchange-mass spectrometry (LX-MS) to study the lipid affinity for membrane proteins on a lipidomic scale. We first mix membrane protein nanodiscs with empty nanodiscs that have no embedded membrane proteins. After allowing lipids to passively exchange between the two populations, we separate the two types of nanodiscs and perform lipidomic analysis on each with liquid chromatography and MS. Enrichment of lipids in the membrane protein nanodiscs reveals the affinity of individual lipids for binding the target membrane protein. We apply this approach to study three membrane proteins. With the Escherichia coli ammonium transporter AmtB and aquaporin AqpZ in nanodiscs with E. coli polar lipid extracts, we detected binding of cardiolipin and phosphatidyl-glycerol lipids to the proteins. With the acetylcholine receptor in nanodiscs with brain polar lipid extracts, we discovered a complex set of lipid interactions that depended on the head group and tail composition. Overall, lipidomic LX-MS provides a detailed understanding of the lipid-binding affinity and thermodynamics for membrane proteins in complex bilayers and provides a unique perspective on the chemical environment surrounding membrane proteins. Lipids can play important roles in modulating membrane protein structure and function. However, it is challenging to identify natural lipids bound to membrane proteins in complex bilayers. Here, we developed lipidomic lipid exchange-mass spectrometry (LX-MS) to study the lipid affinity for membrane proteins on a lipidomic scale. We first mix membrane protein nanodiscs with empty nanodiscs that have no embedded membrane proteins. After allowing lipids to passively exchange between the two populations, we separate the two types of nanodiscs and perform lipidomic analysis on each with liquid chromatography and MS. Enrichment of lipids in the membrane protein nanodiscs reveals the affinity of individual lipids for binding the target membrane protein. We apply this approach to study three membrane proteins. With the ammonium transporter AmtB and aquaporin AqpZ in nanodiscs with polar lipid extracts, we detected binding of cardiolipin and phosphatidyl-glycerol lipids to the proteins. With the acetylcholine receptor in nanodiscs with brain polar lipid extracts, we discovered a complex set of lipid interactions that depended on the head group and tail composition. Overall, lipidomic LX-MS provides a detailed understanding of the lipid-binding affinity and thermodynamics for membrane proteins in complex bilayers and provides a unique perspective on the chemical environment surrounding membrane proteins. |
| Author | Marty, Michael T. Odenkirk, Melanie T. Janczak, Colleen M. Richardson, Kevin Zhang, Guozhi Lee, Ray Wang, Zhihan Aspinwall, Craig A. |
| AuthorAffiliation | Department of Chemistry and Biochemistry Scintillation Nanotechnologies, Inc Bio5 Institute |
| AuthorAffiliation_xml | – name: Scintillation Nanotechnologies, Inc – name: Bio5 Institute – name: Department of Chemistry and Biochemistry – name: 2 Bio5 Institute, University of Arizona, Tucson, AZ, 85721, USA – name: 3 Scintillation Nanotechnologies, Inc., Tucson, AZ, 85721, USA – name: 1 Department of Chemistry and Biochemistry, University of Arizona, Tucson, AZ, 85721, USA |
| Author_xml | – sequence: 1 givenname: Guozhi surname: Zhang fullname: Zhang, Guozhi organization: Department of Chemistry and Biochemistry – sequence: 2 givenname: Melanie T. surname: Odenkirk fullname: Odenkirk, Melanie T. organization: Bio5 Institute – sequence: 3 givenname: Colleen M. surname: Janczak fullname: Janczak, Colleen M. organization: Scintillation Nanotechnologies, Inc – sequence: 4 givenname: Ray surname: Lee fullname: Lee, Ray organization: Scintillation Nanotechnologies, Inc – sequence: 5 givenname: Kevin surname: Richardson fullname: Richardson, Kevin organization: Scintillation Nanotechnologies, Inc – sequence: 6 givenname: Zhihan surname: Wang fullname: Wang, Zhihan organization: Department of Chemistry and Biochemistry – sequence: 7 givenname: Craig A. orcidid: 0000-0002-4359-5812 surname: Aspinwall fullname: Aspinwall, Craig A. organization: Bio5 Institute – sequence: 8 givenname: Michael T. orcidid: 0000-0001-8115-1772 surname: Marty fullname: Marty, Michael T. email: mtmarty@arizona.edu organization: Bio5 Institute |
| BackLink | https://www.ncbi.nlm.nih.gov/pubmed/37700579$$D View this record in MEDLINE/PubMed |
| BookMark | eNptUctuEzEUtVARTVt2rNEsWTDttT1-zAqhqrSRUoEEXVse25M4ytjBdoDs-If-IV_CpEkLSKzu69xzH-cEHYUYHEKvMJxjIPhiqU0-pwaYlPQZmmBGoGaY8CM0AQBSC8npMTrJeTmGDZH4BTqmQgAw0U6QnloXiu-3PsyrWzd0SQdXfUqxOB9-_byf-bW31TQUl7QpPoZcffdlUT3k4-DN3quufpiFDnNX3-qcq89rZ0qKgytpe4ae93qV3cuDPUV3H66-XN7Us4_X08v3s1pTCaU2LWmbxljeUyq6VgDRlrYMrNZWgiXONlwwy3ELnaG9lIy1pBEd6Tjn2ll6it7tedebbnDWjGclvVLr5Aedtipqr_6tBL9Q8_hNYWANNAJGhjcHhhS_blwuavDZuNVqfEncZEUkbziWROAR-nYPNSnmnFz_NAeD2smidrKogywj_PXfuz2BH3X4M3rXtYybFMZX_Z_rN7tLmwM |
| CitedBy_id | crossref_primary_10_1016_j_sbi_2024_102844 crossref_primary_10_1038_s41467_023_44366_w crossref_primary_10_1002_cplu_202300678 crossref_primary_10_1016_j_bbamcr_2024_119784 crossref_primary_10_1016_j_isci_2024_109382 |
| Cites_doi | 10.1016/j.jmb.2021.167105 10.1021/nn103098m 10.1016/j.bbamem.2008.01.015 10.1021/acs.analchem.0c00786 10.1038/nsmb.3195 10.1021/acsanm.8b02136 10.1073/pnas.94.15.8202 10.1038/s41467-017-02397-0 10.1016/j.bbamem.2018.10.017 10.1085/jgp.201711875 10.1021/jacs.8b11529 10.1021/ja9017013 10.1021/bi00521a026 10.1038/nchem.2172 10.1016/S0005-2736(03)00056-7 10.26434/chemrxiv-22023-vd26432d26432 10.1021/acs.chemrev.8b00451 10.1146/annurev-biophys-070816-033620 10.1038/nrm2330 10.1038/s42003-021-01711-3 10.1002/anie.201713167 10.1016/j.bbamem.2015.03.010 10.1021/acs.analchem.2c01488 10.1093/glycob/cwab046 10.1016/0014-5793(90)81288-Y 10.1146/annurev-biophys-070816-033843 10.1016/j.chembiol.2018.03.011 10.1016/S0896-6273(02)00725-0 10.1038/nature13419 10.1073/pnas.1719813115 10.1523/JNEUROSCI.21-02-00504.2001 10.1038/s41580-022-00524-4 10.1016/j.bbamem.2007.10.019 10.1039/C8CC02003E 10.1111/j.1471-4159.2007.04561.x 10.3389/fphys.2021.798102 10.1016/bs.mie.2020.12.003 10.1021/bi00293a012 10.1007/s13361-019-02174-x 10.1002/anie.201709657 10.1021/jacs.6b01771 10.1021/acs.analchem.1c03181 |
| ContentType | Journal Article |
| Copyright | 2023 American Chemical Society |
| Copyright_xml | – notice: 2023 American Chemical Society |
| DBID | CGR CUY CVF ECM EIF NPM AAYXX CITATION 7X8 5PM |
| DOI | 10.1021/jacs.3c05883 |
| DatabaseName | Medline MEDLINE MEDLINE (Ovid) MEDLINE MEDLINE PubMed CrossRef MEDLINE - Academic PubMed Central (Full Participant titles) |
| DatabaseTitle | MEDLINE Medline Complete MEDLINE with Full Text PubMed MEDLINE (Ovid) CrossRef MEDLINE - Academic |
| DatabaseTitleList | MEDLINE - Academic MEDLINE |
| Database_xml | – sequence: 1 dbid: ECM name: MEDLINE url: https://search.ebscohost.com/login.aspx?direct=true&db=cmedm&site=ehost-live sourceTypes: Index Database |
| DeliveryMethod | fulltext_linktorsrc |
| Discipline | Chemistry |
| EISSN | 1520-5126 |
| EndPage | 20867 |
| ExternalDocumentID | 10_1021_jacs_3c05883 37700579 a478448719 |
| Genre | Research Support, U.S. Gov't, Non-P.H.S Journal Article Research Support, N.I.H., Extramural |
| GrantInformation_xml | – fundername: NIGMS NIH HHS grantid: R35 GM128624 |
| GroupedDBID | --- -DZ -ET -~X .DC .K2 4.4 55A 5GY 5RE 5VS 7~N 85S AABXI ABFRP ABHMW ABMVS ABPPZ ABPTK ABQRX ABUCX ACGFO ACGFS ACJ ACNCT ACS ADHLV AEESW AENEX AFEFF AGHSJ AGXLV AHGAQ ALMA_UNASSIGNED_HOLDINGS AQSVZ BAANH BKOMP CS3 DU5 EBS ED~ F5P GGK GNL IH2 IH9 JG~ LG6 P2P ROL RXW TAE TAF TN5 UHB UI2 UKR UPT VF5 VG9 VQA W1F WH7 XSW YQT YZZ ZCA ~02 53G AAHBH ABJNI ACBEA CGR CUPRZ CUY CVF ECM EIF NPM AAYXX CITATION 7X8 5PM |
| ID | FETCH-LOGICAL-a380t-c92944cd6f337b9702ad3950daad80d2ed4675d6190bc3f88559247b2b666aed3 |
| IEDL.DBID | ACS |
| ISSN | 0002-7863 1520-5126 |
| IngestDate | Sat Sep 28 05:38:36 EDT 2024 Sat Oct 26 02:03:21 EDT 2024 Fri Aug 23 01:00:29 EDT 2024 Sat Nov 02 12:32:10 EDT 2024 Thu Sep 28 04:37:39 EDT 2023 |
| IsPeerReviewed | true |
| IsScholarly | true |
| Issue | 38 |
| Language | English |
| LinkModel | DirectLink |
| MergedId | FETCHMERGED-LOGICAL-a380t-c92944cd6f337b9702ad3950daad80d2ed4675d6190bc3f88559247b2b666aed3 |
| Notes | ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23 Authors GZ and MTO contributed equally to this work. Author Contributions |
| ORCID | 0000-0002-4359-5812 0000-0001-8115-1772 |
| PMID | 37700579 |
| PQID | 2864618271 |
| PQPubID | 23479 |
| PageCount | 9 |
| ParticipantIDs | pubmedcentral_primary_oai_pubmedcentral_nih_gov_10540470 proquest_miscellaneous_2864618271 crossref_primary_10_1021_jacs_3c05883 pubmed_primary_37700579 acs_journals_10_1021_jacs_3c05883 |
| PublicationCentury | 2000 |
| PublicationDate | 2023-09-27 |
| PublicationDateYYYYMMDD | 2023-09-27 |
| PublicationDate_xml | – month: 09 year: 2023 text: 2023-09-27 day: 27 |
| PublicationDecade | 2020 |
| PublicationPlace | United States |
| PublicationPlace_xml | – name: United States |
| PublicationTitle | Journal of the American Chemical Society |
| PublicationTitleAlternate | J. Am. Chem. Soc |
| PublicationYear | 2023 |
| 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 ref5/cit5 ref31/cit31 ref2/cit2 ref34/cit34 ref37/cit37 ref28/cit28 ref40/cit40 ref20/cit20 ref17/cit17 ref10/cit10 ref26/cit26 ref35/cit35 ref19/cit19 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 ref7/cit7 |
| References_xml | – ident: ref7/cit7 doi: 10.1016/j.jmb.2021.167105 – ident: ref35/cit35 doi: 10.1021/nn103098m – ident: ref9/cit9 doi: 10.1016/j.bbamem.2008.01.015 – ident: ref8/cit8 doi: 10.1021/acs.analchem.0c00786 – ident: ref11/cit11 doi: 10.1038/nsmb.3195 – ident: ref29/cit29 doi: 10.1021/acsanm.8b02136 – ident: ref30/cit30 doi: 10.1073/pnas.94.15.8202 – ident: ref21/cit21 doi: 10.1038/s41467-017-02397-0 – ident: ref16/cit16 doi: 10.1016/j.bbamem.2018.10.017 – ident: ref2/cit2 doi: 10.1085/jgp.201711875 – ident: ref23/cit23 doi: 10.1021/jacs.8b11529 – ident: ref26/cit26 doi: 10.1021/ja9017013 – ident: ref39/cit39 doi: 10.1021/bi00521a026 – ident: ref14/cit14 doi: 10.1038/nchem.2172 – ident: ref37/cit37 doi: 10.1016/S0005-2736(03)00056-7 – ident: ref20/cit20 doi: 10.26434/chemrxiv-22023-vd26432d26432 – ident: ref5/cit5 doi: 10.1021/acs.chemrev.8b00451 – ident: ref10/cit10 doi: 10.1146/annurev-biophys-070816-033620 – ident: ref1/cit1 doi: 10.1038/nrm2330 – ident: ref19/cit19 doi: 10.1038/s42003-021-01711-3 – ident: ref13/cit13 doi: 10.1002/anie.201713167 – ident: ref27/cit27 doi: 10.1016/j.bbamem.2015.03.010 – ident: ref18/cit18 doi: 10.1021/acs.analchem.2c01488 – ident: ref34/cit34 doi: 10.1093/glycob/cwab046 – ident: ref38/cit38 doi: 10.1016/0014-5793(90)81288-Y – ident: ref3/cit3 doi: 10.1146/annurev-biophys-070816-033843 – ident: ref15/cit15 doi: 10.1016/j.chembiol.2018.03.011 – ident: ref6/cit6 doi: 10.1016/S0896-6273(02)00725-0 – ident: ref22/cit22 doi: 10.1038/nature13419 – ident: ref41/cit41 doi: 10.1073/pnas.1719813115 – ident: ref33/cit33 doi: 10.1523/JNEUROSCI.21-02-00504.2001 – ident: ref4/cit4 doi: 10.1038/s41580-022-00524-4 – ident: ref32/cit32 doi: 10.1016/j.bbamem.2007.10.019 – ident: ref12/cit12 doi: 10.1039/C8CC02003E – ident: ref31/cit31 doi: 10.1111/j.1471-4159.2007.04561.x – ident: ref28/cit28 doi: 10.3389/fphys.2021.798102 – ident: ref24/cit24 doi: 10.1016/bs.mie.2020.12.003 – ident: ref42/cit42 doi: 10.1021/bi00293a012 – ident: ref36/cit36 doi: 10.1007/s13361-019-02174-x – ident: ref17/cit17 doi: 10.1002/anie.201709657 – ident: ref40/cit40 doi: 10.1021/jacs.6b01771 – ident: ref25/cit25 doi: 10.1021/acs.analchem.1c03181 |
| SSID | ssj0004281 |
| Score | 2.5117955 |
| Snippet | Lipids can play important roles in modulating membrane protein structure and function. However, it is challenging to identify natural lipids bound to membrane... |
| SourceID | pubmedcentral proquest crossref pubmed acs |
| SourceType | Open Access Repository Aggregation Database Index Database Publisher |
| StartPage | 20859 |
| SubjectTerms | Cation Transport Proteins Escherichia coli Escherichia coli Proteins Lipidomics Mass Spectrometry Membrane Lipids Membrane Proteins |
| Title | Identifying Membrane Protein–Lipid Interactions with Lipidomic Lipid Exchange-Mass Spectrometry |
| URI | http://dx.doi.org/10.1021/jacs.3c05883 https://www.ncbi.nlm.nih.gov/pubmed/37700579 https://www.proquest.com/docview/2864618271 https://pubmed.ncbi.nlm.nih.gov/PMC10540470 |
| Volume | 145 |
| hasFullText | 1 |
| inHoldings | 1 |
| isFullTextHit | |
| isPrint | |
| link | http://sdu.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwjV3JTsMwEB1ROMCFfSmbjATcghzbjd0jKq16ASEBErcosR3RAykircSRf-AP-RJmkhRoUSVukeMkzowTv7H93gCcKht57V0YCI_wTWXtMECc7AOpSMybe5kkxHfu3-mbR3PVJZmc8zkr-IL0gWxxIS1vGSMbsCQ0ggSCQJ27H_6jMOEE5moTyXqD--zVNADZYnoA-oMqZzdH_hptemv_bec6rNZ4kl1WHWADFny-CcudSRq3LUgqKm5JZ2LX_hmj49yzW5JnGOSf7x-UvNqxcmKw4jgUjOZmWVlOlOXqiHXfKo5wcI1wm1Ha-hEpHeAztuGh173v9IM6r0KQSMNHgUVIpJR1USalTtuai8TJdos79IvhTniHf8-Ww9CKp1ZmxmDUIZRORYqxTuKd3IHFfJj7PWCRFpkiLitPlXKqZZxHwChsxlWStZ1twgmaJa6_iyIul7wFhhxUWhurCWcTh8QvlcTGnHonE2_FaENa2ECDDcdFLEykIgyUdNiE3cp733eS2DYi3DbBTPn1uwLpa0-fyQdPpc52SHBWab7_j5c4gBVKRE87SYQ-hMXR69gfQaNw4-Oyr34BjRHlkA |
| link.rule.ids | 230,315,782,786,887,2769,27085,27933,27934,56747,56797 |
| linkProvider | American Chemical Society |
| linkToHtml | http://sdu.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwlV3JTsMwEB2xHODCvpTVSHCM5NhO7B5RKSqiRUiAxC1KYkdwICDSShz5B_6QL2EmC6UgJLhFjpM4M078xvZ7A3Co0tBpZ31POIRvKmv7HuJk50lFYt7cyTgmvnPvSl_cmpMuyeR4DRcGG1HgnYpyEX-sLkAyQVgoUx4YI6dhNggRBxMS6lyNaZDC-A3a1SaU9T7371fTOJQWk-PQD3D5fY_kl0HndPGfzV2ChRpdsuOqOyzDlMtXYK7TJHVbhbgi5pbkJjZwDxgr545dkljDff7--kaprC0rpwkrxkPBaKaWleVEYK6OWPelYgx7AwTfjJLYD0n3AJ-xBjen3etOz6uzLHixNHzopQiQlEptmEmpk7bmIrayHXCLXjLcCmfxXxpYDLR4ksrMGIxBhNKJSDDyiZ2V6zCTP-ZuE1ioRaaI2coTpawKjHUIH0WacRVnbZu24ADNEtVfSRGVC-ACAxAqrY3VgqPGL9FTJbjxS72DxmkR2pCWOdBgj6MiEiZUIYZN2m_BRuXEzztJbBvRb1tgJtz7WYHUtifP5Pd3peq2T-BWab71h5fYh7ne9aAf9c8uzrdhnlLU0x4ToXdgZvg8crswXdjRXtl9PwCseO39 |
| linkToPdf | http://sdu.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwnV3LSsQwFL34AHXj-zE-I-iykCZpky5lnEHxgaCCu9I2Kbqwip0Bl_6Df-iXeG8f6iiCuCtpmqa5SXNuknMuwJ7KQqed9T3hEL6pPPI9xMnOk4rEvLmTSUJ856NLfX5jDnskk-O3XBisRIklldUmPo3qR5s3CgMkFYQ3ZMYDY-Q4TAahjsjfOuheflIhhfFbxKtNKJuz7t-fprkoK0fnoh8A8_s5yS8TT3_uH1Weh9kGZbKDulsswJgrFmG62wZ3W4KkJuhWJCd25u7RZy4cuyDRhrvi7eWVQlpbVi0X1syHktGKLavSichcX7Hec80c9s4QhDMKZj8g_QN8xzJc93tX3SOvibbgJdLwgZchUFIqs2EupU4jzUViZRRwi9Yy3Apn8Z8aWHS4eJrJ3Bj0RYTSqUjRA0qclSswUTwUbg1YqEWuiOHKU6WsCox1CCNFlnOV5JHNOrCLzRI3o6WMq41wgY4IpTaN1YH91jbxYy288Uu-3dZwMbYhbXdggz0My1iYUIXoPmm_A6u1IT9Kklg3ouF2wIyY-CMDqW6P3inubiv1bZ9ArtJ8_Q8fsQNTF4f9-PT4_GQDZihSPR01EXoTJgZPQ7cF46Udblc9-B1lfvCA |
| 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=Identifying+Membrane+Protein-Lipid+Interactions+with+Lipidomic+Lipid+Exchange-Mass+Spectrometry&rft.jtitle=Journal+of+the+American+Chemical+Society&rft.au=Zhang%2C+Guozhi&rft.au=Odenkirk%2C+Melanie+T&rft.au=Janczak%2C+Colleen+M&rft.au=Lee%2C+Ray&rft.date=2023-09-27&rft.issn=1520-5126&rft.eissn=1520-5126&rft.volume=145&rft.issue=38&rft.spage=20859&rft_id=info:doi/10.1021%2Fjacs.3c05883&rft.externalDBID=NO_FULL_TEXT |
| thumbnail_l | http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/lc.gif&issn=0002-7863&client=summon |
| thumbnail_m | http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/mc.gif&issn=0002-7863&client=summon |
| thumbnail_s | http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/sc.gif&issn=0002-7863&client=summon |