_id,doi,title
14835,10.1002/ange.202219314,"Der starre Kern und die flexible Oberfläche von Amyloidfibrillen – Magic‐Angle‐Spinning NMR Spektroskopie von aromatischen Resten"
14847,10.1039/bk9781839165986-00136,"Preparing Chaperone–Client Protein Complexes for Biophysical and Structural Studies"
14861,10.1002/anie.202304138,"Cover Picture: The rigid core and flexible surface of amyloid fibrils probed by Magic‐Angle‐Spinning NMR spectroscopy of aromatic residues"
13095,10.1021/jacs.3c01200,Disulfide-bond-induced structural frustration and dynamic disorder in a peroxiredoxin from MAS NMR
13096,10.1038/s41586-023-05991-z,Structural basis of NINJ1-mediated plasma membrane rupture in cell death
14036,10.1016/j.sbi.2023.102660,Protein dynamics detected by magic-angle spinning relaxation dispersion NMR
12114,10.1016/j.yjsbx.2022.100079,Aromatic ring flips in differently packed ubiquitin protein crystals from MAS NMR and MD
12497,10.15479/AT:ISTA:12497,Research data to: The rigid core and flexible surface of amyloid fibrils probed by magic-angle-spinning NMR spectroscopy of aromatic residues
12675,10.1002/anie.202219314,"The rigid core and flexible surface of amyloid fibrils probed by Magic‐Angle Spinning NMR of aromatic residues"
12820,10.15479/AT:ISTA:12820,"Research data of the publication ""Disulfide-bond-induced structural frustration and dynamic disorder in a peroxiredoxin from MAS NMR"""
11179,10.1038/s41467-022-29423-0,Functional control of a 0.5 MDa TET aminopeptidase by a flexible loop revealed by MAS NMR
10323,10.3389/fmolb.2021.762005,How do chaperones bind (partly) unfolded client proteins?