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 2.705
Times Cited 21
Arabidopsis / Cultured plant cells, genes pda01294 pda00345 pda01847 pda13139