Prof. Dr. Volker Dötsch

Institute for Biophysical Chemistry
Room N230/103
Max von Laue-Str. 9
60438 Frankfurt am Main
Tel.: +49 69 798 29631
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Research interest

  • characterization of the transcription factor p63
  • membrane proteins
  • molecular basis for autophagy

Main methods

  • Liquid State NMR
  • Cell-free protein production
  • genetic engineering
  • high-throughput robotics

Selected recent publications:

Please clic here for full list of publications.

Intrinsic aggregation propensity of the p63 and p73 TI domains correlates with p53R175H interaction and suggests further significance of aggregation events in the p53 family

Kehrloesser S, Osterburg C, Tuppi M, Schäfer B, Vousden KH, Dötsch V., Cell Death Differ. 2016 Dec;23(12):1952-1960.

Mechanism of TAp73 inhibition by ΔNp63 and structural basis of p63/p73 hetero-tetramerization

Gebel J, Luh LM, Coutandin D, Osterburg C, Löhr F, Schäfer B, Frombach AS, Sumyk M, Buchner L, Krojer T, Salah E, Mathea S, Güntert P, Knapp S, Dötsch V.,  Cell Death Differ. 2016 Dec;23(12):1930-1940.

From Nanodiscs to Isotropic Bicelles: A Procedure for Solution Nuclear Magnetic Resonance Studies of Detergent-Sensitive Integral Membrane Proteins

Laguerre A, Löhr F, Henrich E, Hoffmann B, Abdul-Manan N, Connolly PJ, Perozo E, Moore JM, Bernhard F, Dötsch V., Structure. 2016 Oct 4;24(10):1830-1841.

The CUE Domain of Cue1 Aligns Growing Ubiquitin Chains with Ubc7 for Rapid Elongation

von Delbrück M, Kniss A, Rogov VV, Pluska L, Bagola K, Löhr F, Güntert P, Sommer T, Dötsch V., Mol Cell. 2016 Jun 16;62(6):918-28.

In-cell NMR and EPR spectroscopy of biomacromolecules

Hänsel R, Luh LM, Corbeski I, Trantirek L, Dötsch V., Angew Chem Int Ed Engl. 2014 Sep 22;53(39):10300-14.

Molecular crowding drives active Pin1 into nonspecific complexes with endogenous proteins prior to substrate recognition

Luh LM, Hänsel R, Löhr F, Kirchner DK, Krauskopf K, Pitzius S, Schäfer B, Tufar P, Corbeski I, Güntert P, Dötsch V., J Am Chem Soc. 2013 Sep 18;135(37):13796-803.