TY  - JOUR
A1  - Hundertmark, Michaela
A1  - Popova, Antoaneta V.
A1  - Rausch, Saskia
A1  - Seckler, Robert
A1  - Hincha, Dirk K.
T1  - Influence of drying on the secondary structure of intrinsically disordered and globular proteins
T2  - Biochemical and biophysical research communications
N2  - 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.
KW  - Desiccation
KW  - CD spectroscopy
KW  - FTIR spectroscopy
KW  - Intrinsically disordered proteins
KW  - LEA proteins
KW  - Protein secondary structure
Y1  - 2012
UR  - https://publishup.uni-potsdam.de/frontdoor/index/index/docId/36207
SN  - 0006-291X
VL  - 417
IS  - 1
SP  - 122
EP  - 128
PB  - Elsevier
CY  - San Diego
ER  -