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  Sampling the conformational space of membrane protein surfaces with the AFM

Scheuring, S., Müller, D. J., Stahlberg, H., Engel, H. A., & Engel, A. (2002). Sampling the conformational space of membrane protein surfaces with the AFM. European Biophysics Journal with Biophysics Letters, 31(3), 172-178.

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

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Free keywords: loops; beta-turns; membrane protein; two-dimensional crystal; energy landscape
 Abstract: The atomic force microscope acquires topographs of single native membrane proteins at subnanometer resolution. Owing to the high signal-to-noise ratio, such images allow the conformational space of membrane protein surfaces to be sampled. This is demonstrated by topographs of porin OrnpF, aquaporin-Z, and bacteriorhodopsin, all recorded at a lateral resolution of <7 &ANGS; and a vertical resolution of &SIM;1 &ANGS;. The amplitudes of the domain movements were estimated from a large number of single molecule topographs and the corresponding energy landscapes calculated. To visualize the motion of protein domains, movies were generated by similarity ranking of the observed protein configurations. Electronic supplementary material to this paper can be obtained by using the Springer Link server located at http://dx.doi.org/10.1007/s00249-001-0197-8.

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Language(s): eng - English
 Dates: 2002-06
 Publication Status: Published in print
 Pages: -
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: eDoc: 15468
ISI: 000176827900002
 Degree: -

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Title: European Biophysics Journal with Biophysics Letters
  Alternative Title : Eur. Biophys. J. Biophys. Lett.
Source Genre: Journal
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Publ. Info: -
Pages: - Volume / Issue: 31 (3) Sequence Number: - Start / End Page: 172 - 178 Identifier: ISSN: 0175-7571