36778
2011
2011
eng
1879
1887
9
7
1808
article
Elsevier
Amsterdam
1
--
--
--
Structural transitions in the intrinsically disordered plant dehydration stress protein LEA7 upon drying are modulated by the presence of membranes
Dehydration stress-related late embryogenesis abundant (LEA) proteins have been found in plants, invertebrates and bacteria. Most LEA proteins are unstructured in solution, but some fold into amphipathic a-helices during drying. The Pfam LEA_4 (Group 3) protein LEA7 from the higher plant Arabidopsis thaliana was predicted to be 87% alpha-helical, while CD spectroscopy showed it to be largely unstructured in solution and only 35% alpha-helical in the dry state. However, the dry protein contained 15% beta-sheets. FTIR spectroscopy revealed the (beta-sheets to be largely due to aggregation. beta-Sheet content was reduced and alpha-helix content increased when LEA7 was dried in the presence of liposomes with secondary structure apparently influenced by lipid composition. Secondary structure was also affected by the presence of membranes in the fully hydrated state. A temperature-induced increase in the flexibility of the dry protein was also only observed in the presence of membranes. Functional interactions of LEA7 with membranes in the dry state were indicated by its influence on the thermotropic phase transitions of the lipids and interactions with the lipid headgroup phosphates.
Biochimica et biophysica acta : Biomembranes
10.1016/j.bbamem.2011.03.009
0005-2736
wos:2011-2013
WOS:000291172100013
Hincha, DK (reprint author), Max Planck Inst Mol Pflanzenphysiol, Muhlenberg 1, D-14476 Potsdam, Germany., hincha@mpimp-golm.mpg.de
University of Potsdam
Antoaneta V. Popova
Michaela Hundertmark
Robert Seckler
Dirk K. Hincha
eng
uncontrolled
Desiccation
eng
uncontrolled
CD spectroscopy
eng
uncontrolled
FTIR spectroscopy
eng
uncontrolled
LEA protein
eng
uncontrolled
Protein-membrane interactions
eng
uncontrolled
Protein secondary structure
Institut für Biochemie und Biologie
Referiert
36207
2012
2012
eng
122
128
7
1
417
article
Elsevier
San Diego
1
--
--
--
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.
Biochemical and biophysical research communications
10.1016/j.bbrc.2011.11.067
0006-291X
wos:2011-2013
WOS:000299491600022
Hincha, DK (reprint author), Max Planck Inst Mol Pflanzenphysiol, Muhlenberg 1, D-14476 Potsdam, Germany., hincha@mpimp-golm.mpg.de
University of Potsdam
Michaela Hundertmark
Antoaneta V. Popova
Saskia Rausch
Robert Seckler
Dirk K. Hincha
eng
uncontrolled
Desiccation
eng
uncontrolled
CD spectroscopy
eng
uncontrolled
FTIR spectroscopy
eng
uncontrolled
Intrinsically disordered proteins
eng
uncontrolled
LEA proteins
eng
uncontrolled
Protein secondary structure
Institut für Biochemie und Biologie
Referiert