Deciphering In-vivo Cross-linking Mass Spectrometry Data for Dynamic Protein Structure Analysis
Abstract Protein structure and protein-protein interactions(PPIs) are crucial for regulating cellular activities required for cell viability and homeostasis. Chemical cross-linking coupled with mass spectrometry(CXMS) has become a versatile tool providing insights into both protein structure with di...
Ausführliche Beschreibung
Gespeichert in:
| Autor*in: |
Zhao, Lili [verfasserIn] |
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| Format: |
E-Artikel |
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| Sprache: |
Englisch |
| Erschienen: |
2022 |
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| Schlagwörter: |
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| Anmerkung: |
© Jilin University, The Editorial Department of Chemical Research in Chinese Universities and Springer-Verlag GmbH 2022 |
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| Übergeordnetes Werk: |
Enthalten in: Chemical Research in Chinese Universities - Jilin University and The Editorial Department of Chemical Research in Chinese Universities, 2012, 38(2022), 3 vom: 17. März, Seite 758-762 |
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| Übergeordnetes Werk: |
volume:38 ; year:2022 ; number:3 ; day:17 ; month:03 ; pages:758-762 |
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10.1007/s40242-022-2037-6 |
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| 520 | |a Abstract Protein structure and protein-protein interactions(PPIs) are crucial for regulating cellular activities required for cell viability and homeostasis. Chemical cross-linking coupled with mass spectrometry(CXMS) has become a versatile tool providing insights into both protein structure with distance restraints and protein-protein interactions with interface sites. Cross-links as the most information-rich data in a CXMS experiment are responsible for the structural model validation and integrative modeling with high throughput and sensitivity. In this work, ensemble refinement of the existing protein structure against the in-vivo cross-linking distance restraints was performed for dynamic protein structure modeling and protein interaction binding interface building in the intracellular environment. These results indicate great potential of in-vivo CXMS data for providing a molecular basis of protein structural dynamics exploration and function performance. | ||
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10.1007/s40242-022-2037-6 doi (DE-627)SPR050743007 (SPR)s40242-022-2037-6-e DE-627 ger DE-627 rakwb eng Zhao, Lili verfasserin aut Deciphering In-vivo Cross-linking Mass Spectrometry Data for Dynamic Protein Structure Analysis 2022 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © Jilin University, The Editorial Department of Chemical Research in Chinese Universities and Springer-Verlag GmbH 2022 Abstract Protein structure and protein-protein interactions(PPIs) are crucial for regulating cellular activities required for cell viability and homeostasis. Chemical cross-linking coupled with mass spectrometry(CXMS) has become a versatile tool providing insights into both protein structure with distance restraints and protein-protein interactions with interface sites. Cross-links as the most information-rich data in a CXMS experiment are responsible for the structural model validation and integrative modeling with high throughput and sensitivity. In this work, ensemble refinement of the existing protein structure against the in-vivo cross-linking distance restraints was performed for dynamic protein structure modeling and protein interaction binding interface building in the intracellular environment. These results indicate great potential of in-vivo CXMS data for providing a molecular basis of protein structural dynamics exploration and function performance. chemical cross-linking (dpeaa)DE-He213 Cross-linking distance restraint (dpeaa)DE-He213 Ensemble refinement (dpeaa)DE-He213 Structural dynamics (dpeaa)DE-He213 Disorder region (dpeaa)DE-He213 Gong, Zhou aut Zhao, Qun aut Zhang, Lihua aut Zhang, Yukui aut Enthalten in Chemical Research in Chinese Universities Jilin University and The Editorial Department of Chemical Research in Chinese Universities, 2012 38(2022), 3 vom: 17. März, Seite 758-762 (DE-627)SPR03290777X nnns volume:38 year:2022 number:3 day:17 month:03 pages:758-762 https://dx.doi.org/10.1007/s40242-022-2037-6 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER AR 38 2022 3 17 03 758-762 |
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10.1007/s40242-022-2037-6 doi (DE-627)SPR050743007 (SPR)s40242-022-2037-6-e DE-627 ger DE-627 rakwb eng Zhao, Lili verfasserin aut Deciphering In-vivo Cross-linking Mass Spectrometry Data for Dynamic Protein Structure Analysis 2022 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © Jilin University, The Editorial Department of Chemical Research in Chinese Universities and Springer-Verlag GmbH 2022 Abstract Protein structure and protein-protein interactions(PPIs) are crucial for regulating cellular activities required for cell viability and homeostasis. Chemical cross-linking coupled with mass spectrometry(CXMS) has become a versatile tool providing insights into both protein structure with distance restraints and protein-protein interactions with interface sites. Cross-links as the most information-rich data in a CXMS experiment are responsible for the structural model validation and integrative modeling with high throughput and sensitivity. In this work, ensemble refinement of the existing protein structure against the in-vivo cross-linking distance restraints was performed for dynamic protein structure modeling and protein interaction binding interface building in the intracellular environment. These results indicate great potential of in-vivo CXMS data for providing a molecular basis of protein structural dynamics exploration and function performance. chemical cross-linking (dpeaa)DE-He213 Cross-linking distance restraint (dpeaa)DE-He213 Ensemble refinement (dpeaa)DE-He213 Structural dynamics (dpeaa)DE-He213 Disorder region (dpeaa)DE-He213 Gong, Zhou aut Zhao, Qun aut Zhang, Lihua aut Zhang, Yukui aut Enthalten in Chemical Research in Chinese Universities Jilin University and The Editorial Department of Chemical Research in Chinese Universities, 2012 38(2022), 3 vom: 17. März, Seite 758-762 (DE-627)SPR03290777X nnns volume:38 year:2022 number:3 day:17 month:03 pages:758-762 https://dx.doi.org/10.1007/s40242-022-2037-6 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER AR 38 2022 3 17 03 758-762 |
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10.1007/s40242-022-2037-6 doi (DE-627)SPR050743007 (SPR)s40242-022-2037-6-e DE-627 ger DE-627 rakwb eng Zhao, Lili verfasserin aut Deciphering In-vivo Cross-linking Mass Spectrometry Data for Dynamic Protein Structure Analysis 2022 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © Jilin University, The Editorial Department of Chemical Research in Chinese Universities and Springer-Verlag GmbH 2022 Abstract Protein structure and protein-protein interactions(PPIs) are crucial for regulating cellular activities required for cell viability and homeostasis. Chemical cross-linking coupled with mass spectrometry(CXMS) has become a versatile tool providing insights into both protein structure with distance restraints and protein-protein interactions with interface sites. Cross-links as the most information-rich data in a CXMS experiment are responsible for the structural model validation and integrative modeling with high throughput and sensitivity. In this work, ensemble refinement of the existing protein structure against the in-vivo cross-linking distance restraints was performed for dynamic protein structure modeling and protein interaction binding interface building in the intracellular environment. These results indicate great potential of in-vivo CXMS data for providing a molecular basis of protein structural dynamics exploration and function performance. chemical cross-linking (dpeaa)DE-He213 Cross-linking distance restraint (dpeaa)DE-He213 Ensemble refinement (dpeaa)DE-He213 Structural dynamics (dpeaa)DE-He213 Disorder region (dpeaa)DE-He213 Gong, Zhou aut Zhao, Qun aut Zhang, Lihua aut Zhang, Yukui aut Enthalten in Chemical Research in Chinese Universities Jilin University and The Editorial Department of Chemical Research in Chinese Universities, 2012 38(2022), 3 vom: 17. März, Seite 758-762 (DE-627)SPR03290777X nnns volume:38 year:2022 number:3 day:17 month:03 pages:758-762 https://dx.doi.org/10.1007/s40242-022-2037-6 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER AR 38 2022 3 17 03 758-762 |
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10.1007/s40242-022-2037-6 doi (DE-627)SPR050743007 (SPR)s40242-022-2037-6-e DE-627 ger DE-627 rakwb eng Zhao, Lili verfasserin aut Deciphering In-vivo Cross-linking Mass Spectrometry Data for Dynamic Protein Structure Analysis 2022 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © Jilin University, The Editorial Department of Chemical Research in Chinese Universities and Springer-Verlag GmbH 2022 Abstract Protein structure and protein-protein interactions(PPIs) are crucial for regulating cellular activities required for cell viability and homeostasis. Chemical cross-linking coupled with mass spectrometry(CXMS) has become a versatile tool providing insights into both protein structure with distance restraints and protein-protein interactions with interface sites. Cross-links as the most information-rich data in a CXMS experiment are responsible for the structural model validation and integrative modeling with high throughput and sensitivity. In this work, ensemble refinement of the existing protein structure against the in-vivo cross-linking distance restraints was performed for dynamic protein structure modeling and protein interaction binding interface building in the intracellular environment. These results indicate great potential of in-vivo CXMS data for providing a molecular basis of protein structural dynamics exploration and function performance. chemical cross-linking (dpeaa)DE-He213 Cross-linking distance restraint (dpeaa)DE-He213 Ensemble refinement (dpeaa)DE-He213 Structural dynamics (dpeaa)DE-He213 Disorder region (dpeaa)DE-He213 Gong, Zhou aut Zhao, Qun aut Zhang, Lihua aut Zhang, Yukui aut Enthalten in Chemical Research in Chinese Universities Jilin University and The Editorial Department of Chemical Research in Chinese Universities, 2012 38(2022), 3 vom: 17. März, Seite 758-762 (DE-627)SPR03290777X nnns volume:38 year:2022 number:3 day:17 month:03 pages:758-762 https://dx.doi.org/10.1007/s40242-022-2037-6 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER AR 38 2022 3 17 03 758-762 |
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10.1007/s40242-022-2037-6 doi (DE-627)SPR050743007 (SPR)s40242-022-2037-6-e DE-627 ger DE-627 rakwb eng Zhao, Lili verfasserin aut Deciphering In-vivo Cross-linking Mass Spectrometry Data for Dynamic Protein Structure Analysis 2022 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © Jilin University, The Editorial Department of Chemical Research in Chinese Universities and Springer-Verlag GmbH 2022 Abstract Protein structure and protein-protein interactions(PPIs) are crucial for regulating cellular activities required for cell viability and homeostasis. Chemical cross-linking coupled with mass spectrometry(CXMS) has become a versatile tool providing insights into both protein structure with distance restraints and protein-protein interactions with interface sites. Cross-links as the most information-rich data in a CXMS experiment are responsible for the structural model validation and integrative modeling with high throughput and sensitivity. In this work, ensemble refinement of the existing protein structure against the in-vivo cross-linking distance restraints was performed for dynamic protein structure modeling and protein interaction binding interface building in the intracellular environment. These results indicate great potential of in-vivo CXMS data for providing a molecular basis of protein structural dynamics exploration and function performance. chemical cross-linking (dpeaa)DE-He213 Cross-linking distance restraint (dpeaa)DE-He213 Ensemble refinement (dpeaa)DE-He213 Structural dynamics (dpeaa)DE-He213 Disorder region (dpeaa)DE-He213 Gong, Zhou aut Zhao, Qun aut Zhang, Lihua aut Zhang, Yukui aut Enthalten in Chemical Research in Chinese Universities Jilin University and The Editorial Department of Chemical Research in Chinese Universities, 2012 38(2022), 3 vom: 17. März, Seite 758-762 (DE-627)SPR03290777X nnns volume:38 year:2022 number:3 day:17 month:03 pages:758-762 https://dx.doi.org/10.1007/s40242-022-2037-6 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER AR 38 2022 3 17 03 758-762 |
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Abstract Protein structure and protein-protein interactions(PPIs) are crucial for regulating cellular activities required for cell viability and homeostasis. Chemical cross-linking coupled with mass spectrometry(CXMS) has become a versatile tool providing insights into both protein structure with distance restraints and protein-protein interactions with interface sites. Cross-links as the most information-rich data in a CXMS experiment are responsible for the structural model validation and integrative modeling with high throughput and sensitivity. In this work, ensemble refinement of the existing protein structure against the in-vivo cross-linking distance restraints was performed for dynamic protein structure modeling and protein interaction binding interface building in the intracellular environment. These results indicate great potential of in-vivo CXMS data for providing a molecular basis of protein structural dynamics exploration and function performance. © Jilin University, The Editorial Department of Chemical Research in Chinese Universities and Springer-Verlag GmbH 2022 |
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Abstract Protein structure and protein-protein interactions(PPIs) are crucial for regulating cellular activities required for cell viability and homeostasis. Chemical cross-linking coupled with mass spectrometry(CXMS) has become a versatile tool providing insights into both protein structure with distance restraints and protein-protein interactions with interface sites. Cross-links as the most information-rich data in a CXMS experiment are responsible for the structural model validation and integrative modeling with high throughput and sensitivity. In this work, ensemble refinement of the existing protein structure against the in-vivo cross-linking distance restraints was performed for dynamic protein structure modeling and protein interaction binding interface building in the intracellular environment. These results indicate great potential of in-vivo CXMS data for providing a molecular basis of protein structural dynamics exploration and function performance. © Jilin University, The Editorial Department of Chemical Research in Chinese Universities and Springer-Verlag GmbH 2022 |
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Abstract Protein structure and protein-protein interactions(PPIs) are crucial for regulating cellular activities required for cell viability and homeostasis. Chemical cross-linking coupled with mass spectrometry(CXMS) has become a versatile tool providing insights into both protein structure with distance restraints and protein-protein interactions with interface sites. Cross-links as the most information-rich data in a CXMS experiment are responsible for the structural model validation and integrative modeling with high throughput and sensitivity. In this work, ensemble refinement of the existing protein structure against the in-vivo cross-linking distance restraints was performed for dynamic protein structure modeling and protein interaction binding interface building in the intracellular environment. These results indicate great potential of in-vivo CXMS data for providing a molecular basis of protein structural dynamics exploration and function performance. © Jilin University, The Editorial Department of Chemical Research in Chinese Universities and Springer-Verlag GmbH 2022 |
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<?xml version="1.0" encoding="UTF-8"?><collection xmlns="http://www.loc.gov/MARC21/slim"><record><leader>01000naa a22002652 4500</leader><controlfield tag="001">SPR050743007</controlfield><controlfield tag="003">DE-627</controlfield><controlfield tag="005">20230507192143.0</controlfield><controlfield tag="007">cr uuu---uuuuu</controlfield><controlfield tag="008">230507s2022 xx |||||o 00| ||eng c</controlfield><datafield tag="024" ind1="7" ind2=" "><subfield code="a">10.1007/s40242-022-2037-6</subfield><subfield code="2">doi</subfield></datafield><datafield tag="035" ind1=" " ind2=" "><subfield code="a">(DE-627)SPR050743007</subfield></datafield><datafield tag="035" ind1=" " ind2=" "><subfield code="a">(SPR)s40242-022-2037-6-e</subfield></datafield><datafield tag="040" ind1=" " ind2=" "><subfield code="a">DE-627</subfield><subfield code="b">ger</subfield><subfield code="c">DE-627</subfield><subfield code="e">rakwb</subfield></datafield><datafield tag="041" ind1=" " ind2=" "><subfield code="a">eng</subfield></datafield><datafield tag="100" ind1="1" ind2=" "><subfield code="a">Zhao, Lili</subfield><subfield code="e">verfasserin</subfield><subfield code="4">aut</subfield></datafield><datafield tag="245" ind1="1" ind2="0"><subfield code="a">Deciphering In-vivo Cross-linking Mass Spectrometry Data for Dynamic Protein Structure Analysis</subfield></datafield><datafield tag="264" ind1=" " ind2="1"><subfield code="c">2022</subfield></datafield><datafield tag="336" ind1=" " ind2=" "><subfield code="a">Text</subfield><subfield code="b">txt</subfield><subfield code="2">rdacontent</subfield></datafield><datafield tag="337" ind1=" " ind2=" "><subfield code="a">Computermedien</subfield><subfield code="b">c</subfield><subfield code="2">rdamedia</subfield></datafield><datafield tag="338" ind1=" " ind2=" "><subfield code="a">Online-Ressource</subfield><subfield code="b">cr</subfield><subfield code="2">rdacarrier</subfield></datafield><datafield tag="500" ind1=" " ind2=" "><subfield code="a">© Jilin University, The Editorial Department of Chemical Research in Chinese Universities and Springer-Verlag GmbH 2022</subfield></datafield><datafield tag="520" ind1=" " ind2=" "><subfield code="a">Abstract Protein structure and protein-protein interactions(PPIs) are crucial for regulating cellular activities required for cell viability and homeostasis. Chemical cross-linking coupled with mass spectrometry(CXMS) has become a versatile tool providing insights into both protein structure with distance restraints and protein-protein interactions with interface sites. Cross-links as the most information-rich data in a CXMS experiment are responsible for the structural model validation and integrative modeling with high throughput and sensitivity. In this work, ensemble refinement of the existing protein structure against the in-vivo cross-linking distance restraints was performed for dynamic protein structure modeling and protein interaction binding interface building in the intracellular environment. These results indicate great potential of in-vivo CXMS data for providing a molecular basis of protein structural dynamics exploration and function performance.</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">chemical cross-linking</subfield><subfield code="7">(dpeaa)DE-He213</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">Cross-linking distance restraint</subfield><subfield code="7">(dpeaa)DE-He213</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">Ensemble refinement</subfield><subfield code="7">(dpeaa)DE-He213</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">Structural dynamics</subfield><subfield code="7">(dpeaa)DE-He213</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">Disorder region</subfield><subfield code="7">(dpeaa)DE-He213</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Gong, Zhou</subfield><subfield code="4">aut</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Zhao, Qun</subfield><subfield code="4">aut</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Zhang, Lihua</subfield><subfield code="4">aut</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Zhang, Yukui</subfield><subfield code="4">aut</subfield></datafield><datafield tag="773" ind1="0" ind2="8"><subfield code="i">Enthalten in</subfield><subfield code="t">Chemical Research in Chinese Universities</subfield><subfield code="d">Jilin University and The Editorial Department of Chemical Research in Chinese Universities, 2012</subfield><subfield code="g">38(2022), 3 vom: 17. 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