Influence of drying on the secondary structure of intrinsically disordered and globular proteins

被引：31

作者：

Hundertmark, Michaela ^{[1
]}

Popova, Antoaneta V. ^{[1
]}

Rausch, Saskia ^{[1
]}

Seckler, Robert ^{[2
]}

Hincha, Dirk K. ^{[1
]}

机构：

[1] Max Planck Inst Mol Pflanzenphysiol, D-14476 Potsdam, Germany

[2] Univ Potsdam, Inst Phys Biochem, D-14476 Potsdam, Germany

来源：

BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | 2012年 / 417卷 / 01期

关键词：

Desiccation; CD spectroscopy; FTIR spectroscopy; Intrinsically disordered proteins; LEA proteins; Protein secondary structure; EMBRYOGENESIS-ABUNDANT PROTEIN; CIRCULAR-DICHROISM; INFRARED-SPECTROSCOPY; GALACTOSYL CYCLITOLS; WATER-STRESS; LEA PROTEIN; PHOSPHATIDYLCHOLINE; TRANSITIONS; OLIGOSACCHARIDES; TEMPERATURE;

D O I：

10.1016/j.bbrc.2011.11.067

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

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. (C) 2011 Elsevier Inc. All rights reserved.

引用

页码：122 / 128

页数：7

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