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Anne Bremer
Researcher at St. Jude Children's Research Hospital
Publications - 27
Citations - 1056
Anne Bremer is an academic researcher from St. Jude Children's Research Hospital. The author has contributed to research in topics: Chemistry & Biology. The author has an hindex of 8, co-authored 14 publications receiving 434 citations. Previous affiliations of Anne Bremer include Max Planck Society.
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Journal ArticleDOI
Valence and patterning of aromatic residues determine the phase behavior of prion-like domains
Erik W. Martin,Alex S. Holehouse,Ivan Peran,Mina Farag,J. Jeremías Incicco,Anne Bremer,Christy R. Grace,Andrea Soranno,Rohit V. Pappu,Tanja Mittag +9 more
TL;DR: It is shown that the numbers (valence) of aromatic residues in PLDs determine the extent of temperature-dependent compaction of individual molecules in dilute solutions, which determines full binodals that quantify concentrations of PLDs within coexisting dilute and dense phases as a function of temperature.
Journal ArticleDOI
How do intrinsically disordered protein regions encode a driving force for liquid–liquid phase separation?
TL;DR: In this paper, a conceptual framework that divides IDRs into interacting and solvating regions has been proposed, and analytical instantiations and coarse-grained models can test their understanding of the driving forces against experimental phase behavior.
Posted Content
How do intrinsically disordered protein regions encode a driving force for liquid-liquid phase separation?
TL;DR: Validated simulation paradigms enable the exploration of sequence space to help the understanding of how disordered protein regions can encode phase behavior, which IDRs may mediate phase separation in cells, and which IDR are in contrast highly soluble.
Journal ArticleDOI
Folding of intrinsically disordered plant LEA proteins is driven by glycerol-induced crowding and the presence of membranes
TL;DR: Two truncated versions of LEA25 are created (2H and 4H) to elucidate the structural and functional significance of this domain, which was important in cryoprotection as the central domain itself only provided a low level of protection.
Journal ArticleDOI
Intrinsically Disordered Stress Protein COR15A Resides at the Membrane Surface during Dehydration
Anne Bremer,Ben Kent,Thomas Hauß,Anja Thalhammer,Nageshwar R. Yepuri,Tamim A. Darwish,Christopher J. Garvey,Gary Bryant,Dirk K. Hincha +8 more
TL;DR: It is shown that COR15A starts to fold into α-helices already under mild dehydration conditions (97% relative humidity (RH), corresponding to freezing at -3°C) and that folding gradually increases with decreasing RH, in agreement with the hypothesis that Cor15A-membrane interaction is at least, in part, driven by a hydrophobic interaction between the lipids and thehydrophobic face of the amphipathic protein α-helix.