1 Early life
2 The Hofmeister series
Early life Hofmeister's father was a doctor in Prague, where Hofmeister first began his studies, under the physiologist Karl Hugo Huppert, himself a student of Carl Lehmann. Hofmeister's Habilitationsschrift in 1879 concerned the peptic products of digestion. Hofmeister became a Professor of Pharmacology at the First Faculty of Medicine, Charles University in Prague in 1885, then eventually moved to Strasbourg in 1896. The Hofmeister series Main article: Hofmeister series Hofmeister discovered a series of salts that have consistent effects on the solubility of proteins and (it was discovered later) on the stability of their secondary and tertiary structure. Anions appear to have a larger effect than cations, and are usually ordered
> H P
> a c e t a t e > C
> C l
> C l
> S C
displaystyle mathrm F^ - approx SO_ 4 ^ 2- >HPO_ 4 ^ 2- >acetate>Cl^ - >NO_ 3 ^ - >Br^ - >ClO_ 3 ^ - >I^ - >ClO_ 4 ^ - >SCN^ -
(This is a partial listing; many more salts have been studied.) The order of cations is usually given as
> g u a n i d i n i u m
displaystyle mathrm NH_ 4 ^ + >K^ + >Na^ + >Li^ + >Mg^ 2+ >Ca^ 2+ >guanidinium
The mechanism of the
Hofmeister series is not entirely clear, but
seems to result mainly from effects on the solvent at higher salt
concentrations (> 100 mM). Early members of the series increase
solvent surface tension and decrease the solubility of nonpolar
molecules (salt out); in effect, they strengthen the hydrophobic
interaction. By contrast, later salts in the series increase the
solubility of nonpolar molecules (salt in) and decrease the order in
water; in effect, they weaken the hydrophobic effect. However, these
salts also interact directly with proteins (which are charged and have
strong dipole moments) and may even bind specifically (e.g., phosphate
and sulfate binding to ribonuclease A). Ions that have a strong
salting in effect such as I− and SCN− are strong denaturants,
because they salt in the peptide group, and thus interact much more
strongly with the unfolded form of a protein than with its native
form. Consequently, they pull the unfolding reaction. Moreover,
they may have direct interactions with some standard hydrophobic
molecules, e.g., benzene.
primary structure peptide bond Picture of Hofmeister at Science and Society site, UK Hofmeister Still Mystifies, Chemical & Engineering News, July 16, 2012.
See also: Hofmeister References
Wikimedia Commons has media related to Franz Hofmeister.
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Zhou, Huan-Xiang (October 2005). "Interactions of macromolecules with
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Works by or about
WorldCat Identities VIAF: 117738948 LCCN: no2010147022 ISNI: 0000 0000 8329 9191 GND: 117526835 SUDOC: 081975902 N