TY  - CHAP
A1  - Stephan, Mareike Sophia
A1  - Barbirz, Stefanie
A1  - Robinson, Tom
A1  - Yandrapalli, Naresh
A1  - Dimova, Rumiana
T1  - Bacterial mimetic systems for studying bacterial inactivation and infection
BT  - Meeting abstract: 65th Annual Meeting of the Biophysical Society (BPS), Feb. 22-26, 2021
T2  - Biophysical journal : BJ / ed. by the Biophysical Society
Y1  - 2021
U6  - https://doi.org/10.1016/j.bpj.2020.11.1087
SN  - 0006-3495
SN  - 1542-0086
VL  - 120
IS  - 3
SP  - 148A
EP  - 148A
PB  - Cell Press
CY  - Cambridge
ER  - 
TY  - THES
A1  - Dimova, Rumiana
T1  - Probing the membrane nanoregime with optical microscopy
Y1  - 2011
CY  - Potsdam
ER  - 
TY  - JOUR
A1  - Hundertmark, Michaela
A1  - Dimova, Rumiana
A1  - Lengefeld, Jan
A1  - Seckler, Robert
A1  - Hincha, Dirk K.
T1  - The intrinsically disordered late embryogenesis abundant protein LEA18 from Arabidopsis thaliana modulates membrane stability through binding and folding.
N2  - Intrinsically disordered proteins (IDPs) constitute a substantial part of cellular proteomes. Late embryogenesis abundant (LEA) proteins are mostly predicted to be IDPs associated with dehydration tolerance in many plant, animal and bacterial species. Their functions, however, are largely unexplored and also their structure and interactions with potential target molecules have only recently been experimentally investigated in a small number of proteins. Here, we report on the structure and interactions with membranes of the Pfam LEA_1 protein LEA18 from the higher plant Arabidopsis thaliana. This functionally uncharacterized positively charged protein specifically aggregated and destabilized negatively charged liposomes. Isothermal titration calorimetry showed binding of the protein to both charged and uncharged membranes. LEA18 alone was largely unstructured in solution. While uncharged membranes had no influence on the secondary structure of LEA18, the protein partially folded into ;-sheet structure in the presence of negatively charged liposomes. These data suggest that LEA18 does not function as a membrane stabilizing protein, as suggested for other LEA proteins. Instead, a possible function of LEA18 could be the composition-dependent modulation of membrane stability, e.g., during signaling or vesicle-mediated transport. Research Highlights
Y1  - 2011
SN  - 0006-3002
ER  -