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  Single proteins observed by atomic force microscopy

Scheuring, S., Fotiadis, D., Möller, C., Müller, S. A., Engel, A., & Müller, D. J. (2001). Single proteins observed by atomic force microscopy. Single Molecules, 2(2), 59-67.

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 Creators:
Scheuring, S., Author
Fotiadis, D., Author
Möller, C.1, Author           
Müller, S. A., Author
Engel, A., Author
Müller, D. J.1, Author           
Affiliations:
1Max Planck Institute of Molecular Cell Biology and Genetics, Max Planck Society, ou_2340692              

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 Abstract: Here we discuss the experimental approaches that have allowed high resolution atomic force microscopy (AFM) imaging, and review results that show AFM to be of great interest for biologists, AFM allows single proteins to be imaged under physiologically relevant conditions. The exceptional signal-to- noise ratio and resolution of AFM topographs enables the oligomerization state and characteristic substructures of individual proteins to be resolved. Several examples demonstrate the capabilities of AFM to directly observe single proteins, and their conformational changes, to study protein- protein interactions and to follow the assembly of membrane proteins. We consider the AFM techniques that have allowed high resolution imaging, and review results that show AFM to be a powerful method to analyze biological processes at the level of single molecules.

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Language(s): eng - English
 Dates: 2001
 Publication Status: Issued
 Pages: -
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: eDoc: 15392
ISI: 000174074500002
 Degree: -

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Title: Single Molecules
  Alternative Title : Single Mol.
Source Genre: Journal
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Pages: - Volume / Issue: 2 (2) Sequence Number: - Start / End Page: 59 - 67 Identifier: ISSN: 1438-5163