M. Sc. Patrick Knox-Brown

Bild: Universität Potsdam


Patrick Knox-Brown

PhD candidate
University of Potsdam
Institute of Biochemistry and Biology
Karl-Liebknecht-Str. 24-25, House 25, B/0.22
14476 Potsdam, DE
Email: knoxbrown@uni-potsdam.de
Phone: 0049-331-977-5244


M.Sc. Biotechnology, 2016, Beuth University of Applied Sciences, Berlin, Germany
B.Sc.  Biotechnology, 2013, Beuth University of Applied Sciences, Berlin, Germany

Research interests

LEA (Late Embryogenesis Abundant) proteins are abiotic stress regulated proteins, which enhance plant survival upon dehydration. My PhD research project should enhance the structural and functional knowledge about COR15A, a member of the LEA_4 family proteins from Arabidopsis thaliana. COR15A is an intrinsically disordered protein in solution but undergoes structural transitions into predominantly α-helical structure upon dehydration, similar to its closely related group members: LEA11 and LEA25. In such a folded state they associate and thereby stabilize membranes. I am investigating target protein folding on different structural levels in response to water deficiency in the presence and absence of membranes, as well as protein-membrane interaction and the resulting effects on membrane organization. It is my goal to find a consensus motif within the three target proteins that can be found in further LEA proteins and held responsible for such a membrane binding and stabilizing effect.

Key methods

Cloning, spectroscopic methods (UV/VIS, CD, FTIR), static and dynamic light scattering



Shou K, Bremer A, Rindfleisch T, Knox-Brown P, Hirai M, Rekas A, Garvey CJ, Hincha DK, Stadler AM, Thalhammer A. Conformational selection of the intrinsically disordered plant stress protein COR15A in response to solution osmolarity - an X-ray and light scattering study. Phys Chem Chem Phys. 2019;21(34):18727-18740

Sowemimo OT, Knox-Brown P, Borcherds W, Rindfleisch T, Thalhammer A, Daughdrill GW. Conserved Glycines Control Disorder and Function in the Cold-Regulated Protein, COR15A. Biomolecules. 2019;9(3). pii: E84

Bild: Universität Potsdam