Der starre Kern und die flexible Oberfläche von Amyloidfibrillen – MagicAngleSpinning NMR Spektroskopie von aromatischen Resten
L.M. Becker, M. Berbon, A. Vallet, A. Grelard, E. Morvan, B. Bardiaux, R. Lichtenecker, M. Ernst, A. Loquet, P. Schanda, Angewandte Chemie 135 (2023).

Preparing Chaperone–Client Protein Complexes for Biophysical and Structural Studies
I. Sudec, P. Schanda, in:, S. Hiller, M. Liu, L. He (Eds.), Biophysics of Molecular Chaperones, Royal Society of Chemistry, 2023, pp. 136–161.

Protein dynamics detected by magic-angle spinning relaxation dispersion NMR
F. Napoli, L.M. Becker, P. Schanda, Current Opinion in Structural Biology 82 (2023).

The rigid core and flexible surface of amyloid fibrils probed by MagicAngle Spinning NMR of aromatic residues
L.M. Becker, M. Berbon, A. Vallet, A. Grelard, E. Morvan, B. Bardiaux, R. Lichtenecker, M. Ernst, A. Loquet, P. Schanda, Angewandte Chemie International Edition 62 (2023).

Functional control of a 0.5 MDa TET aminopeptidase by a flexible loop revealed by MAS NMR
D.F. Gauto, P. Macek, D. Malinverni, H. Fraga, M. Paloni, I. Sudec, A. Hessel, J.P. Bustamante, A. Barducci, P. Schanda, Nature Communications 13 (2022).

How do chaperones bind (partly) unfolded client proteins?
I. Sudec, B. Bersch, P. Schanda, Frontiers in Molecular Biosciences 8 (2021).