Biomolecular NMR Spectroscopy:
Dance of Molecules

We mourn the passing of Dr. Matthias Görlach.

Matthias Görlach worked as a research group leader from 1994 to 2015. From 2015 until his retirement he headed the core and service facilities. Even after his retirement in February 2021, he remained connected to the FLI as a consultant.

Matthias Görlach died after a long, serious illness on March 15th, 2023. The FLI and its employees owe a great deal to Matthias Görlach. As a molecular biologist who mastered the technology of protein characterization at the highest scientific level, he reorganized the entire research infrastructure at the FLI in 2014/15 and drove its professionalization. He was the ombudsman at FLI for many years and championed a culture of scientific integrity. In doing so, he always enjoyed the trust of his colleagues - as an experienced scientist with an immense detailed knowledge and as an extremely prudent and communicative person. In his undertakings, he always combined pragmatism, optimism and consideration. "I am on a diplomatic mission," is how he himself described his approach.

Matthias Görlach worked tirelessly in both research and scientific organization for the benefit of our institute. His death tears a painful gap, but his achievements will also be felt and visible in the future. For his significant contribution to the development of our institute over many years, he deserves our esteem, respect and thanks.

We will always honor his memory.

From January 2016 to February 2021, Dr. Matthias Görlach headed the Core Facilities and Scientific Services at FLI as Head of Core. Prior to that, he led the research group Biomolecular NMR Spectroscopy at FLI.

Research theme of the former NMR group

Accumulation of molecular damage and decreasing repair capacity constitutes a typical phenotype of aging cells and tissues. The group focused on structural integrity of and specific recognition mechanisms between biomolecules. Deficiency in proteins involved in DNA replication or repair causes genomic damage and may lead to premature aging syndromes. Moreover, protein damage accumulation via stochastic chemical modifications (e.g. by reactive oxygen species) and/or proteolytic (mis-) processing may promote ill-folding and/or aggregation of proteins. This in turn may trigger pleiotropic responses such as a compromised general capacity of protein turn-over and/or compromised signaling pathways. As consequence, cellular malfunction and eventually tissue degeneration is observed.

The aim was to mechanistically understand the consequences of molecular damage and the related mechanisms of genome maintenance and repair as well as of protein aggregation. To this end, the three-dimensional structure and function of DNA replication and repair proteins of heme-binding proteins and of Alzheimer's associated amyloid aggregates were addressed.

A part of this research is continued in the Core Facilities Proteomics and Bioinformatics and the core service unit Protein Production, respectively.