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  In vivo folding efficiencies for mutants of the P22 tailspike beta-helix protein correlate with predicted stability changes

Reich, L., Becker, M., Seckler, R., & Weikl, T. R. (2009). In vivo folding efficiencies for mutants of the P22 tailspike beta-helix protein correlate with predicted stability changes. Biophysical Chemistry, 141(2-3), 186-192.

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Item Permalink: https://hdl.handle.net/11858/00-001M-0000-0015-4FE6-7 Version Permalink: https://hdl.handle.net/11858/00-001M-0000-0015-4FE7-5
Genre: Journal Article

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429821.pdf (Publisher version), 801KB
 
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 Creators:
Reich, L.1, Author           
Becker, M.2, Author
Seckler, R., Author
Weikl, T. R.3, Author           
Affiliations:
1Theorie & Bio-Systeme, Max Planck Institute of Colloids and Interfaces, Max Planck Society, ou_1863289              
2Max Planck Society, ou_persistent13              
3Thomas Weikl, Theorie & Bio-Systeme, Max Planck Institute of Colloids and Interfaces, Max Planck Society, ou_1863330              

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Free keywords: Repeat proteins; beta-helix; Protein stability; Mutational analysis; Energy landscape
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Language(s): eng - English
 Dates: 2009-05
 Publication Status: Issued
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 Rev. Type: Peer
 Identifiers: eDoc: 429821
ISI: 000265168400008
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Title: Biophysical Chemistry
  Alternative Title : Biophys. Chem.
Source Genre: Journal
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Pages: - Volume / Issue: 141 (2-3) Sequence Number: - Start / End Page: 186 - 192 Identifier: ISSN: 0301-4622