| RRC ID |
21126
|
| Author |
Hundertmark M, Popova AV, Rausch S, Seckler R, Hincha DK.
|
| Title |
Influence of drying on the secondary structure of intrinsically disordered and globular proteins.
|
| Journal |
Biochem Biophys Res Commun
|
| Abstract |
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.
|
| Volume |
417(1)
|
| Pages |
122-8
|
| Published |
2012-1-6
|
| DOI |
10.1016/j.bbrc.2011.11.067
|
| PII |
S0006-291X(11)02081-X
|
| PMID |
22155233
|
| MeSH |
Amino Acid Sequence
Arabidopsis Proteins / chemistry*
Carbohydrates / chemistry
Circular Dichroism
Desiccation
Lactoglobulins / chemistry*
Molecular Sequence Data
Oligosaccharides / chemistry
Plant Proteins / chemistry*
Protein Folding
Protein Structure, Secondary
Ribonuclease, Pancreatic / chemistry*
Serum Albumin, Bovine / chemistry*
Solubility
Solutions
Spectroscopy, Fourier Transform Infrared
|
| IF |
2.985
|
| Times Cited |
27
|
|
WOS Category
|
BIOPHYSICS
BIOCHEMISTRY & MOLECULAR BIOLOGY
|
| Resource |
| Arabidopsis / Cultured plant cells, genes |
pda01294 pda00345 pda01847 pda13139 |
