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Reentrant liquid condensate phase of proteins is stabilized by hydrophobic and non-ionic interactions
View ORCID ProfileGeorg Krainer, View ORCID ProfileTimothy J. Welsh, View ORCID ProfileJerelle A. Joseph, Jorge R. Espinosa, Ella de Csilléry, Akshay Sridhar, Zenon Toprakcioglu, Giedre Gudiškytė, Magdalena A. Czekalska, William E. Arter, Peter St George-Hyslop, View ORCID ProfileRosana Collepardo-Guevara, View ORCID ProfileSimon Alberti, View ORCID ProfileTuomas P.J. Knowles
doi: https://doi.org/10.1101/2020.05.04.076299
Georg Krainer
1Centre for Misfolding Diseases, Department of Chemistry, University of Cambridge, Lensfield Road, Cambridge CB2 1EW, UK
Timothy J. Welsh
1Centre for Misfolding Diseases, Department of Chemistry, University of Cambridge, Lensfield Road, Cambridge CB2 1EW, UK
Jerelle A. Joseph
2Cavendish Laboratory, Department of Physics, University of Cambridge, J J Thomson Avenue, Cambridge CB3 0HE, UK
3Department of Genetics, University of Cambridge, Cambridge CB2 3EH, UK
4Department of Chemistry, University of Cambridge, Lensfield Road, Cambridge CB2 1EW, UK
Jorge R. Espinosa
2Cavendish Laboratory, Department of Physics, University of Cambridge, J J Thomson Avenue, Cambridge CB3 0HE, UK
3Department of Genetics, University of Cambridge, Cambridge CB2 3EH, UK
4Department of Chemistry, University of Cambridge, Lensfield Road, Cambridge CB2 1EW, UK
Ella de Csilléry
1Centre for Misfolding Diseases, Department of Chemistry, University of Cambridge, Lensfield Road, Cambridge CB2 1EW, UK
Akshay Sridhar
2Cavendish Laboratory, Department of Physics, University of Cambridge, J J Thomson Avenue, Cambridge CB3 0HE, UK
3Department of Genetics, University of Cambridge, Cambridge CB2 3EH, UK
4Department of Chemistry, University of Cambridge, Lensfield Road, Cambridge CB2 1EW, UK
Zenon Toprakcioglu
1Centre for Misfolding Diseases, Department of Chemistry, University of Cambridge, Lensfield Road, Cambridge CB2 1EW, UK
Giedre Gudiškytė
1Centre for Misfolding Diseases, Department of Chemistry, University of Cambridge, Lensfield Road, Cambridge CB2 1EW, UK
Magdalena A. Czekalska
1Centre for Misfolding Diseases, Department of Chemistry, University of Cambridge, Lensfield Road, Cambridge CB2 1EW, UK
William E. Arter
1Centre for Misfolding Diseases, Department of Chemistry, University of Cambridge, Lensfield Road, Cambridge CB2 1EW, UK
Peter St George-Hyslop
5Cambridge Institute for Medical Research, Department of Clinical Neurosciences, University of Cambridge, Cambridge CB2 0XY, UK; Department of Medicine (Division of Neurology), University of Toronto and University Health Network, Toronto, Ontario M5S 3H2, Canada
Rosana Collepardo-Guevara
2Cavendish Laboratory, Department of Physics, University of Cambridge, J J Thomson Avenue, Cambridge CB3 0HE, UK
3Department of Genetics, University of Cambridge, Cambridge CB2 3EH, UK
4Department of Chemistry, University of Cambridge, Lensfield Road, Cambridge CB2 1EW, UK
Simon Alberti
6Biotechnology Center (BIOTEC), Center for Molecular and Cellular Bioengineering (CMCB), Technische Universität Dresden, Tatzberg 47/49, 01307 Dresden, Germany
Tuomas P.J. Knowles
1Centre for Misfolding Diseases, Department of Chemistry, University of Cambridge, Lensfield Road, Cambridge CB2 1EW, UK
2Cavendish Laboratory, Department of Physics, University of Cambridge, J J Thomson Avenue, Cambridge CB3 0HE, UK
Posted May 07, 2020.
Reentrant liquid condensate phase of proteins is stabilized by hydrophobic and non-ionic interactions
Georg Krainer, Timothy J. Welsh, Jerelle A. Joseph, Jorge R. Espinosa, Ella de Csilléry, Akshay Sridhar, Zenon Toprakcioglu, Giedre Gudiškytė, Magdalena A. Czekalska, William E. Arter, Peter St George-Hyslop, Rosana Collepardo-Guevara, Simon Alberti, Tuomas P.J. Knowles
bioRxiv 2020.05.04.076299; doi: https://doi.org/10.1101/2020.05.04.076299
Reentrant liquid condensate phase of proteins is stabilized by hydrophobic and non-ionic interactions
Georg Krainer, Timothy J. Welsh, Jerelle A. Joseph, Jorge R. Espinosa, Ella de Csilléry, Akshay Sridhar, Zenon Toprakcioglu, Giedre Gudiškytė, Magdalena A. Czekalska, William E. Arter, Peter St George-Hyslop, Rosana Collepardo-Guevara, Simon Alberti, Tuomas P.J. Knowles
bioRxiv 2020.05.04.076299; doi: https://doi.org/10.1101/2020.05.04.076299
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