Klaus Roman Liedl

This study identifies the Dsc ubiquitin ligase complex as a quality control mechanism at the Golgi that degrades orphaned proteins by assessing transmembrane domain hydrophobicity.

The paper investigates how asymmetric conformational changes in CaV1.3 channels mediate voltage- and calcium-dependent inactivation through distinct molecular mechanisms.

This study identifies that the Arabian camel's IgA isotype expresses both unconventional single-domain and canonical heavy chains, similar to IgG, expanding the immunoglobulin repertoire.

The paper highlights challenges in antibody structure prediction, emphasizing structural inaccuracies and introducing a tool to validate models.

OCD.py calculates inter-domain orientations for all immunoglobulin domains using a transferable approach, applicable to both single structures and molecular dynamics trajectories.

The paper determines the NMR structures of four Cor a 1 isoforms and shows that structural flexibility inversely correlates with IgE-binding potential.