English
 
Help Privacy Policy Disclaimer
  Advanced SearchBrowse

Item

ITEM ACTIONSEXPORT
Add to Basket
  Local TagsRelease HistoryDetailsSummary

Released
Journal Article

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

MPS-Authors
/persons/resource/persons192051

D'Imprima,  Edoardo
Department of Structural Biology, Max Planck Institute of Biophysics, Max Planck Society;

/persons/resource/persons232073

Floris,  Davide
Department of Structural Biology, Max Planck Institute of Biophysics, Max Planck Society;

/persons/resource/persons213903

Sánchez,  Ricardo
Sofja Kovalevskaja Group, Max Planck Institute of Biophysics, Max Planck Society;

/persons/resource/persons137764

Kühlbrandt,  Werner       
Department of Structural Biology, Max Planck Institute of Biophysics, Max Planck Society;

External Resource
No external resources are shared
Fulltext (restricted access)
There are currently no full texts shared for your IP range.
Fulltext (public)
There are no public fulltexts stored in PuRe
Supplementary Material (public)
There is no public supplementary material available
Citation

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.


Cite as: https://hdl.handle.net/21.11116/0000-0003-5474-C
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.