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Influence of drying on the secondary structure of intrinsically disordered and globular proteins

  • Circular dichroism (CD) spectroscopy of five Arabidopsis late embryogenesis abundant (LEA) proteins constituting the plant specific families LEA_5 and LEA_6 showed that they are intrinsically disordered in solution and partially fold during drying. Structural predictions were comparable to these results for hydrated LEA_6, but not for LEA_5 proteins. FTIR spectroscopy showed that verbascose, but not sucrose, strongly affected the structure of the dry proteins. The four investigated globular proteins were only mildly affected by drying in the absence, but strongly in the presence of sugars. These data highlight the larger structural flexibility of disordered compared to globular proteins and the impact of sugars on the structure of both disordered and globular proteins during drying.

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Metadaten
Author:Michaela Hundertmark, Antoaneta V. Popova, Saskia Rausch, Robert SecklerORCiDGND, Dirk K. Hincha
DOI:https://doi.org/10.1016/j.bbrc.2011.11.067
ISSN:0006-291X (print)
Parent Title (English):Biochemical and biophysical research communications
Publisher:Elsevier
Place of publication:San Diego
Document Type:Article
Language:English
Year of first Publication:2012
Year of Completion:2012
Release Date:2017/03/26
Tag:CD spectroscopy; Desiccation; FTIR spectroscopy; Intrinsically disordered proteins; LEA proteins; Protein secondary structure
Volume:417
Issue:1
Pagenumber:7
First Page:122
Last Page:128
Funder:University of Potsdam
Organizational units:Mathematisch-Naturwissenschaftliche Fakultät / Institut für Biochemie und Biologie
Peer Review:Referiert