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  Intrinsically Disordered p53 and Its Complexes Populate Compact Conformations in the Gas Phase

Pagel, K., Natan, E., Hall, Z., Fersht, A. R., & Robinson, C. V. (2013). Intrinsically Disordered p53 and Its Complexes Populate Compact Conformations in the Gas Phase. Angewandte Chemie International Edition: a journal of the Gesellschaft Deutscher Chemiker, 52(1), 361-365. doi:10.1002/anie.201203047.

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 Creators:
Pagel, Kevin1, 2, Author           
Natan, Eviatar3, Author
Hall, Zoe2, Author
Fersht, Alan R.3, Author
Robinson, Carol V.2, Author
Affiliations:
1Molecular Physics, Fritz Haber Institute, Max Planck Society, ou_634545              
2Physical & Theoretical Chemistry Laboratory, Department of Chemistry, University of Oxford, South Parks Road, OX1 3QZ, Oxford (UK), ou_persistent22              
3MRC Laboratory of Molecular Biology, Hills Road, CB2 0QH, Cambridge (UK), ou_persistent22              

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Free keywords: analytical methods; disordered proteins; ion mobility; mass spectrometry; protein folding
 Abstract: Spontaneous shrinking: The intrinsically disordered tumor suppressor protein p53 was analyzed by using a combination of ion mobility mass spectrometry and molecular dynamics simulations. Structured p53 subdomains retain their overall topology upon transfer into the gas phase. When intrinsically disordered segments are introduced into the protein sequence, however, the complex spontaneously collapses in the gas phase to a compact conformation.

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Language(s): eng - English
 Dates: 2012-04-202012-05-162012-07-092013-01-02
 Publication Status: Issued
 Pages: 5
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: DOI: 10.1002/anie.201203047
 Degree: -

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Title: Angewandte Chemie International Edition : a journal of the Gesellschaft Deutscher Chemiker
Source Genre: Journal
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Publ. Info: Weinheim/Bergstr. : Verlag Chemie
Pages: - Volume / Issue: 52 (1) Sequence Number: - Start / End Page: 361 - 365 Identifier: ISSN: 0570-0833
CoNE: https://pure.mpg.de/cone/journals/resource/110984073528720