Hofmeister, Franz

Hofmeister, Franz (1850-1922), physiological chemist and pioneer of protein structure. He succeeded Hoppe-Seyler at Strasbourg, where he led a productive research school. Franz Hofineister and EmU Fischer exerted both, each in his own way, a significant influence on the development of the biochemical sciences. Already in 1902, at a historical meeting at Karlsbad, Franz Hofineister first formulated scientifically the assumption of an amide-like linkage of the individual amino acids in proteins, four years before Fischer coined the term peptide [F. Hofmeister, Naturw. Rdsch. 1902, 17, 529]. 

Geison, "Scientific Change." J. S. Fruton, "Contrasts in Scientific Style Emil Fischer and Franz Hofmeister, Their Research Schools and Their Theories of Protein Structure," Proceedings of the American Philosophical Society 129 (1985) 313370 also see, Fruton, "The Liebig Research Group, a Reappraisal," ibid., 132 (1988) 166 Holmes, "Complementarity," 121164 and J. B. Morrell, "The Chemist Breeders ... 

Fruton, Joseph S. "Contrasts in Scientific Style Emil Fischer and Franz Hofmeister Their Research Schools and Their Theories of Protein Structure." Proceedings of the American Philosophical Society 129 (1985) 313370. 

The second aspect refers to the protein nature of enzymes. In 1894 Fischer (Fischer, 1909) stated that amongst the agents which serve the living cell the proteins are the most important. He was convinced that enzymes are proteins. The role of this key problem may be illustrated with a citation from Fruton (1979) ... the peptide theory was indeed only a hypothesis fifty years after Franz Hofmeister and Emil Fischer advanced it... (in 1902). The nature and stracture of proteins remained unknown throughout the 19th century remarkably, technological applications were nevertheless put into practice since the middle of the century (see above), based on their action, eventually recognized as catalysis, only. 

W. Kunz, J. Hendle, and B. W. Ninham. Zur Lehre von der Wirkung der Salze (about the science of the effect of salts). Franz Hofmeister s historical papers. Curr. Opin. Colloid Interface Sci., 9 19-37, 2004. 

The scale is currently known as the Hofmeister (or lyotropic) series to honor Franz Hofmeister, who described the effects of salts on a variety of physiological samples and ranked salts in a sequence that later proved universal. The series of papers he wrote more than a century ago were recently translated into English [22]. Hofmeister simply introduced the concept of ranking salts based on common cations and anions. In this context, it is pertinent to underline that Hofmeister categorically stated that the effect of a salt depends on both its anion and cation. Hofmeister s results were subsequently extrapolated to produce the ion-specific series not connected to... 

This empirical series arises fiorri experiments done in 1888 by the Austro-German chemist Franz Hofmeister (1850-1922). who was interested in the relative effectiveness of different salts in precipitating proteins from egg while. The alternative name lyotropic series, derives from the Greek meaning roughly pertaining to solvent aflinily"... 

Plate. 22. Franz Hofmeister (1850-1922), (Fischer, biograph. Lexikon)... 

Franz Hofmeister, Archiv fur experimentelle Pathologic und Pharmakologie, 1888, xxiv, 247 1889, XXV, i 1891, xxviii, 210 long abstr. in Z. phys. Chem., 1888, ii, 860 Meyer and Dunkel, Z.phys. Chem.y 1931, Bodenstein Festband, 553. 

In 1902 Franz Hofmeister knew that the ultimate products of protein digestion are amino acids. Native proteins, Hofmeister said, have little free amino nitrogen, but large amounts appear on hydrolysis. Compounds containing the peptide bond give the biuret reaction, and so do condensation products of amino acids. Therefore, Hofmeister said ... 

Most popular is Franz Hofmeister s work carried out essentially in the 1880s and 1890s in... 

Atomistic molecular dynamics simulations reveal a detailed molecular view of electrolyte solutions and interfaces that goes far beyond simple continuum theories. This view has been started with studies of the air/water interface and is currently extended to more complex solid interfaces, colloidal systems, and back to biopolymer solutions, where the whole endeavor of ion specificity began with the classical studies of Franz Hofmeister. Quantum chemical simulations, which have the potential to give more reliable predictions of ion density profiles than classical force field simulations, become increasingly feasible with increasing computational resources [9]. 

The replacement of tissue protein by food protein did not seem possible if the latter were metabolized and excreted as urea, uric acid and COg. Although some amino acids had been isolated, little was known about protein structure at that time. It was only in 1902 that Emil Fischer and Franz Hofmeister independently demonstrated the occurrence of the peptide linkage in protein. 

---