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  Protein denaturation at the air-water interface and how to prevent it

D'Imprima, E., Floris, D., Joppe, M., Sánchez, R., Grinninger, M., & Kühlbrandt, W. (2019). Protein denaturation at the air-water interface and how to prevent it. eLife, 8: e42747. doi:10.7554/eLife.42747.

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 Creators:
D'Imprima, Edoardo1, Author           
Floris, Davide1, Author           
Joppe, Mirko2, Author
Sánchez, Ricardo3, Author           
Grinninger, Martin2, Author
Kühlbrandt, Werner1, Author           
Affiliations:
1Department of Structural Biology, Max Planck Institute of Biophysics, Max Planck Society, ou_2068291              
2Buchmann Institute for Molecular Life Sciences, Institute of Organic Chemistry and Chemical Biology, Goethe University Frankfurt, Frankfurt, Germany, ou_persistent22              
3Sofja Kovalevskaja Group, Max Planck Institute of Biophysics, Max Planck Society, ou_2253651              

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Free keywords: CryoEM; CryoET; Graphene; Protein denaturation; S. cerevisiae; molecular biophysics; structural biology
 Abstract: Electron cryo-microscopy analyzes the structure of proteins and protein complexes in vitrified solution. Proteins tend to adsorb to the air-water interface in unsupported films of aqueous solution, which can result in partial or complete denaturation. We investigated the structure of yeast fatty acid synthase at the air-water interface by electron cryo-tomography and single-particle image processing. Around 90% of complexes adsorbed to the air-water interface are partly denatured. We show that the unfolded regions face the air-water interface. Denaturation by contact with air may happen at any stage of specimen preparation. Denaturation at the air-water interface is completely avoided when the complex is plunge-frozen on a substrate of hydrophilized graphene.

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Language(s): eng - English
 Dates: 2018-10-102019-02-272019-04-01
 Publication Status: Published online
 Pages: 18
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: DOI: 10.7554/eLife.42747
 Degree: -

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Title: eLife
Source Genre: Journal
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Publ. Info: Cambridge : eLife Sciences Publications
Pages: - Volume / Issue: 8 Sequence Number: e42747 Start / End Page: - Identifier: ISSN: 2050-084X
CoNE: https://pure.mpg.de/cone/journals/resource/2050-084X