English
 
Help Privacy Policy Disclaimer
  Advanced SearchBrowse

Item

ITEM ACTIONSEXPORT
  Stabilization of Dry Sucrose Glasses by Four LEA_4 Proteins from Arabidopsis thaliana

Hincha, D. K., Zuther, E., & Popova, A. V. (2021). Stabilization of Dry Sucrose Glasses by Four LEA_4 Proteins from Arabidopsis thaliana. Biomolecules, 11(5): 615. doi:10.3390/biom11050615.

Item is

Basic

show hide
Genre: Journal Article

Files

show Files

Locators

show
hide
Locator:
Link (Any fulltext)
Description:
-

Creators

show
hide
 Creators:
Hincha, D. K.1, Author              
Zuther, E.1, Author              
Popova, Antoaneta V.2, Author
Affiliations:
1Transcript Profiling, Infrastructure Groups and Service Units, Max Planck Institute of Molecular Plant Physiology, Max Planck Society, ou_1753306              
2External Organizations, ou_persistent22              

Content

show
hide
Free keywords: -
 Abstract: Cells of many organisms and organs can withstand an (almost) total water loss (anhydrobiosis). Sugars play an essential role in desiccation tolerance due to their glass formation ability during dehydration. In addition, intrinsically disordered LEA proteins contribute to cellular survival under such conditions. One possible mechanism of LEA protein function is the stabilization of sugar glasses. However, little is known about the underlying mechanisms. Here we used FTIR spectroscopy to investigate sucrose (Suc) glass stability dried from water or from two buffer components in the presence of four recombinant LEA and globular reference proteins. Buffer ions influenced the strength of the Suc glass in the order Suc lt; Suc/Tris lt; Suc/NaP. LEA proteins strengthened the sugar H-bonded network and the molecular structure in the glassy state. The position of νOH peak and the wavenumber–temperature coefficient (WTCg) provided similar information about the H-bonded network. Protein aggregation of LEA proteins was reduced in the desiccation-induced Suc glassy state. Detailed knowledge about the role of LEA proteins in the stabilization of dry sugar glasses yields information about their role in anhydrobiosis. This may open the possibility to use such proteins in biotechnical applications requiring dry storage of biologicals such as proteins, cells or tissues.

Details

show
hide
Language(s): eng - English
 Dates: 2021
 Publication Status: Published in print
 Pages: -
 Publishing info: -
 Table of Contents: -
 Rev. Type: -
 Identifiers: DOI: 10.3390/biom11050615
BibTex Citekey: biom11050615
 Degree: -

Event

show

Legal Case

show

Project information

show

Source 1

show
hide
Title: Biomolecules
Source Genre: Journal
 Creator(s):
Affiliations:
Publ. Info: Basel, Switzerland : MDPI
Pages: - Volume / Issue: 11 (5) Sequence Number: 615 Start / End Page: - Identifier: ISSN: 2218-273X
CoNE: https://pure.mpg.de/cone/journals/resource/2218-273X