TY  - JOUR
A1  - Navarro-Retamal, Carlos
A1  - Bremer, Anne
A1  - Alzate-Morales, Jans H.
A1  - Caballero, Julio
A1  - Hincha, Dirk K.
A1  - Gonzalez, Wendy
A1  - Thalhammer, Anja
T1  - Molecular dynamics simulations and CD spectroscopy reveal hydration-induced unfolding of the intrinsically disordered LEA proteins COR15A and COR15B from Arabidopsis thaliana
JF  - Physical chemistry, chemical physics : a journal of European Chemical Societies
N2  - The LEA (late embryogenesis abundant) proteins COR15A and COR15B from Arabidopsis thaliana are intrinsically disordered under fully hydrated conditions, but obtain alpha-helical structure during dehydration, which is reversible upon rehydration. To understand this unusual structural transition, both proteins were investigated by circular dichroism (CD) and molecular dynamics (MD) approaches. MD simulations showed unfolding of the proteins in water, in agreement with CD data obtained with both HIS-tagged and untagged recombinant proteins. Mainly intramolecular hydrogen bonds (H-bonds) formed by the protein backbone were replaced by H-bonds with water molecules. As COR15 proteins function in vivo as protectants in leaves partially dehydrated by freezing, unfolding was further assessed under crowded conditions. Glycerol reduced (40%) or prevented (100%) unfolding during MD simulations, in agreement with CD spectroscopy results. H-bonding analysis indicated that preferential exclusion of glycerol from the protein backbone increased stability of the folded state.
Y1  - 2016
U6  - https://doi.org/10.1039/c6cp02272c
SN  - 1463-9076
SN  - 1463-9084
VL  - 18
SP  - 25806
EP  - 25816
PB  - Royal Society of Chemistry
CY  - Cambridge
ER  - 
TY  - GEN
A1  - Navarro-Retamal, Carlos
A1  - Bremer, Anne
A1  - Alzate-Morales, Jans H.
A1  - Caballero, Julio
A1  - Hincha, Dirk K.
A1  - González, Wendy
A1  - Thalhammer, Anja
T1  - Molecular dynamics simulations and CD spectroscopy reveal hydration-induced unfolding of the intrinsically disordered LEA proteins COR15A and COR15B from Arabidopsis thaliana
N2  - The LEA (late embryogenesis abundant) proteins COR15A and COR15B from Arabidopsis thaliana are intrinsically disordered under fully hydrated conditions, but obtain α-helical structure during dehydration, which is reversible upon rehydration. To understand this unusual structural transition, both proteins were investigated by circular dichroism (CD) and molecular dynamics (MD) approaches. MD simulations showed unfolding of the proteins in water, in agreement with CD data obtained with both HIS-tagged and untagged recombinant proteins. Mainly intramolecular hydrogen bonds (H-bonds) formed by the protein backbone were replaced by H-bonds with water molecules. As COR15 proteins function in vivo as protectants in leaves partially dehydrated by freezing, unfolding was further assessed under crowded conditions. Glycerol reduced (40%) or prevented (100%) unfolding during MD simulations, in agreement with CD spectroscopy results. H-bonding analysis indicated that preferential exclusion of glycerol from the protein backbone increased stability of the folded state.
T3  - Zweitveröffentlichungen der Universität Potsdam : Mathematisch-Naturwissenschaftliche Reihe - 321 
Y1  - 2016
U6  - http://nbn-resolving.de/urn/resolver.pl?urn:nbn:de:kobv:517-opus4-394503
SP  - 25806
EP  - 25816
ER  - 
TY  - JOUR
A1  - Hilker, Monika
A1  - Schwachtje, Jens
A1  - Baier, Margarete
A1  - Balazadeh, Salma
A1  - Bäurle, Isabel
A1  - Geiselhardt, Sven
A1  - Hincha, Dirk K.
A1  - Kunze, Reinhard
A1  - Mueller-Roeber, Bernd
A1  - Rillig, Matthias G.
A1  - Rolff, Jens
A1  - Schmülling, Thomas
A1  - Steppuhn, Anke
A1  - van Dongen, Joost
A1  - Whitcomb, Sarah J.
A1  - Wurst, Susanne
A1  - Zuther, Ellen
A1  - Kopka, Joachim
T1  - Priming and memory of stress responses in organisms lacking a nervous system
JF  - Biological reviews
KW  - priming
KW  - stress signalling
KW  - epigenetics
KW  - memory
KW  - fitness
KW  - stress tolerance
KW  - defence
KW  - bet hedging
Y1  - 2016
U6  - https://doi.org/10.1111/brv.12215
SN  - 1464-7931
SN  - 1469-185X
VL  - 91
SP  - 1118
EP  - 1133
PB  - Wiley-Blackwell
CY  - Hoboken
ER  -