Nanoparticles and photochemistry for native-like transmembrane protein footprinting
The intrinsic flexibility of membranes proteins still poses a challenge in determining their active structure. Here the authors describe the development of a method that combines chemical footprinting and mass spectrometry to assist in determining the structure of native membrane proteins and their...
| Main Authors: | , , , , , |
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| Format: | Article |
| Language: | English |
| Published: |
Nature Portfolio
2021-12-01
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| Series: | Nature Communications |
| Online Access: | https://doi.org/10.1038/s41467-021-27588-8 |
| _version_ | 1818873514462019584 |
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| author | Jie Sun Xiaoran Roger Liu Shuang Li Peng He Weikai Li Michael L. Gross |
| author_facet | Jie Sun Xiaoran Roger Liu Shuang Li Peng He Weikai Li Michael L. Gross |
| author_sort | Jie Sun |
| collection | DOAJ |
| description | The intrinsic flexibility of membranes proteins still poses a challenge in determining their active structure. Here the authors describe the development of a method that combines chemical footprinting and mass spectrometry to assist in determining the structure of native membrane proteins and their dynamics. |
| first_indexed | 2024-12-19T12:55:55Z |
| format | Article |
| id | doaj.art-79f9a105291b4eca88c2f9f488f9ee6d |
| institution | Directory Open Access Journal |
| issn | 2041-1723 |
| language | English |
| last_indexed | 2024-12-19T12:55:55Z |
| publishDate | 2021-12-01 |
| publisher | Nature Portfolio |
| record_format | Article |
| series | Nature Communications |
| spelling | doaj.art-79f9a105291b4eca88c2f9f488f9ee6d2022-12-21T20:20:24ZengNature PortfolioNature Communications2041-17232021-12-0112111010.1038/s41467-021-27588-8Nanoparticles and photochemistry for native-like transmembrane protein footprintingJie Sun0Xiaoran Roger Liu1Shuang Li2Peng He3Weikai Li4Michael L. Gross5Department of Chemistry, Washington University in St. LouisDepartment of Chemistry, Washington University in St. LouisDepartment of Biochemistry and Molecular Biophysics, Washington University School of MedicineDepartment of Biochemistry and Molecular Biophysics, Washington University School of MedicineDepartment of Biochemistry and Molecular Biophysics, Washington University School of MedicineDepartment of Chemistry, Washington University in St. LouisThe intrinsic flexibility of membranes proteins still poses a challenge in determining their active structure. Here the authors describe the development of a method that combines chemical footprinting and mass spectrometry to assist in determining the structure of native membrane proteins and their dynamics.https://doi.org/10.1038/s41467-021-27588-8 |
| spellingShingle | Jie Sun Xiaoran Roger Liu Shuang Li Peng He Weikai Li Michael L. Gross Nanoparticles and photochemistry for native-like transmembrane protein footprinting Nature Communications |
| title | Nanoparticles and photochemistry for native-like transmembrane protein footprinting |
| title_full | Nanoparticles and photochemistry for native-like transmembrane protein footprinting |
| title_fullStr | Nanoparticles and photochemistry for native-like transmembrane protein footprinting |
| title_full_unstemmed | Nanoparticles and photochemistry for native-like transmembrane protein footprinting |
| title_short | Nanoparticles and photochemistry for native-like transmembrane protein footprinting |
| title_sort | nanoparticles and photochemistry for native like transmembrane protein footprinting |
| url | https://doi.org/10.1038/s41467-021-27588-8 |
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