Dictionary of Scientific Biography Vol 18. Supplement 2. by Charles Coulston Gillispie (ed.) Frederic L. Holmes (editor

By Charles Coulston Gillispie (ed.) Frederic L. Holmes (editor in chief)

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Extra resources for Dictionary of Scientific Biography Vol 18. Supplement 2. ALEKSANDR NIKOLAEVICH LEBEDEV - FRITZ ZWICKY

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Lang recognized from the beginning that the distribution of charges in such an assembly of macromolecules must be statistical . At a given moment a particular molecule may carry a net charge Z ; but all the molecules are constantly exchanging protons with the solvent, and the value of Z for any individual molecule is constantly fluctuating . Hence the charge as mea s ured from the titration curve is a mean value, Z, averaged over all the molecules in the system . Later Lang showed, in his Dunham lectures at Harvard Medical School (1939), that the standard deviation of Z is directly related to the steepness of the titration curve, which gives Z as a function of pH at any point : (1) dZ/dln(H+) = - ItKa) where e is the proton charge, D is the dielectric constant of the solvent, k is Boltzmann's constant, and K is the reciprocal mean distance of the ion atmosphere around the central protein ion in the Debye-Huckel theory .

Tiselius, in Biographical Memoirs of Fellows of the Royal Society, 6 (1960), 157-168_ NOTES I . K . Linderstr¢m-Lang, "S . P . L . " in Comptes renc/us des travaux du Laboratoire Carlsberg . serie chirnique, 23 (1939), i-xxi ; see xi . 2 . For later developments in this field, derived from LinderstomLang's work, see R . Keith Cannan, "The Acid-Base Titration of Proteins," in Chemical Reviews, 30 (1942), 395-412 ; and Charles Tanford, "The Interpretation of Hydrogen Ion Titration Curves of Proteins," in Advances in Protein Chemistry, 17 (1962), 69-165 .

He pictured the attack of proteolytic enzymes on the protein as involving a process that, in its simplest form, could be written as This shrinkage in volume is due primarily to electrostriction ; the electric field around the ions produced by the hydrolysis causes the surrounding polar water molecules to become oriented around the ions and to pack more tightly together . Using dilatometers, Lang and Jacobsen followed the volume change that occurred with 33-lactoglobulin hydrolyzed by trypsin or chymotrypsin, correlating the volume change with the number of bonds broken by the enzyme .

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