The memorial plaque of Franz Hofmeister (1850, Prague - 1922, Würzburg) was installed on the building where the professor (1885) and later dean of the Faculty of Medicine was the head of the then Prague Pharmacological Institute and where he also conducted his experiments with protein isolation. The black stone plaque with a portrait relief medallion of the scientist, a gilded autograph below the medallion and the Hofmeister series of ions in the chemical formula is accompanied by an embossed seal of Charles University. The plaque is the work of sculptor Milan Knobloch (1921-2020) and was cast by Oldřich Hejtmánek and his co-workers. The plaque includes a Czech-German text with a chemical summary formula in a cast font:
Chemist Prof. Franz Hofmeister (1850-1922) worked in this building,
who predicted that amino acids are linked in proteins by peptide
and who proposed the lyotropic (Hofmeister) series of ions in 1888.
C4H4O62- > SO42- > HPO42- > C3H5O (CO2)33- >
CH3CO2- > HCO3- > CrO42- > CL- > NO3- > CLO3-
In diesem Gebäude forschte der berühmte Chemiker
prof. Franz Hofmeister (1850–1922), welcher die Peptidbindungen
der Aminosäuren in Eiweissen vorhersagta und 1888 die Lyotropische
(Hofmeister) Reihe der Ionen Vorschlug.
Together with the unveiling of a commemorative plaque in honour of the 160th anniversary of the birth of this eminent Prague native, an international symposium was prepared in cooperation with the University of Reich at the Vila Lanna in Prague (October 2010).
Franz Hofmeister was born into the family of a prominent Prague surgeon. He completed his medical studies in 1874. After his appointment as a full professor (1884), he became the head of the Prague Pharmacological Institute and de facto the first experimental pharmacologist in the Austrian monarchy. Together with the German chemist Emil H. L. Fischer, recipient of the Nobel Prize in Chemistry (1902), co-discovered) the peptide bond by which amino acids in proteins are joined together. In October 1896 he left for the post of doctor and head of the institute of physiological chemistry in Strasbourg, where he was twice elected dean of the Strasbourg medical faculty and where he continued his experiments. His last years after 1919 were spent at the Faculty of Medicine in Würzburg.
Professor Hofmeister was the first researcher to look systematically at the effect of salts on proteins and found a number of their abilities - for example, table salt (sodium chloride) lies somewhere in the middle of this range of protein precipitation abilities. In addition, Hofmeister also concentrated on a series of anions with a common cation and vice versa, thus being able to separate a series of ions and cations to proteins.
The result of his continuous experimentation is the so-called lyotropic, Hofmeister series of ions, aligned according to their ability to solubilize proteins from water solution. Over time, this definition has been shown to apply to many other biological, chemical and physical processes in water solutions. To this day, however, there is no molecular model that fully explains it.
Unfortunately, the physics of the Hofmeister series of ions has not yet been proven and clarified. In general, it is an ingenious simplification, and the exceptions to its validity point to the complex nature of biochemical interactions.
