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.
Author details: | Michaela Hundertmark, Antoaneta V. Popova, Saskia Rausch, Robert SecklerORCiDGND, Dirk K. HinchaORCiDGND |
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DOI: | https://doi.org/10.1016/j.bbrc.2011.11.067 |
ISSN: | 0006-291X |
Title of parent work (English): | Biochemical and biophysical research communications |
Publisher: | Elsevier |
Place of publishing: | San Diego |
Publication type: | Article |
Language: | English |
Year of first publication: | 2012 |
Publication year: | 2012 |
Release date: | 2017/03/26 |
Tag: | CD spectroscopy; Desiccation; FTIR spectroscopy; Intrinsically disordered proteins; LEA proteins; Protein secondary structure |
Volume: | 417 |
Issue: | 1 |
Number of pages: | 7 |
First page: | 122 |
Last Page: | 128 |
Funding institution: | University of Potsdam |
Organizational units: | Mathematisch-Naturwissenschaftliche Fakultät / Institut für Biochemie und Biologie |
Peer review: | Referiert |