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  Dual energy landscape: The functional state of the β-barrel outer membrane protein G molds its unfolding energy landscape

Damaghi, M., Sapra, K. T., Köster, S., Yildiz, Ö., Kühlrandt, W., & Muller, D. J. (2010). Dual energy landscape: The functional state of the β-barrel outer membrane protein G molds its unfolding energy landscape. Proteomics, 10(23), 4151-4162.

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Item Permalink: https://hdl.handle.net/11858/00-001M-0000-0024-D6F8-1 Version Permalink: https://hdl.handle.net/11858/00-001M-0000-0024-D6F9-0
Genre: Journal Article

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 Creators:
Damaghi, Mehdi, Author
Sapra, K. Tanuj, Author
Köster, Stefan1, Author           
Yildiz, Özkan1, Author           
Kühlrandt, Werner1, Author           
Muller, Daniel J., Author
Affiliations:
1Department of Structural Biology, Max Planck Institute of Biophysics, Max Planck Society, ou_2068291              

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Free keywords: Atomic force microscopy; Interactions; Mechanical properties; Nanoproteomics; pH gating; Single-molecule force spectroscopy
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Language(s): eng - English
 Dates: 2010
 Publication Status: Issued
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 Rev. Type: Peer
 Identifiers: eDoc: 521536
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Title: Proteomics
  Alternative Title : Proteomics
Source Genre: Journal
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Pages: - Volume / Issue: 10 (23) Sequence Number: - Start / End Page: 4151 - 4162 Identifier: -