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By Alton Meister

Advances in Enzymology and similar components of Molecular Biology is a seminal sequence within the box of biochemistry, providing researchers entry to authoritative reports of the most recent discoveries in all components of enzymology and molecular biology. those landmark volumes date again to 1941, offering an unequalled view of the historic improvement of enzymology. The sequence deals researchers the most recent knowing of enzymes, their mechanisms, reactions and evolution, roles in complicated organic approach, and their program in either the laboratory and undefined. every one quantity within the sequence good points contributions through best pioneers and investigators within the box from world wide. All articles are conscientiously edited to make sure thoroughness, caliber, and clarity.

With its wide variety of subject matters and lengthy ancient pedigree, Advances in Enzymology and comparable components of Molecular Biology can be utilized not just via scholars and researchers in molecular biology, biochemistry, and enzymology, but in addition by means of any scientist drawn to the invention of an enzyme, its homes, and its functions.

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Stretched rubber contracts when the temperature is raised; as heat is absorhed the entropy increases ( b Q / T = bS) and a more random distribution of the links of the chain molecules occurs. Ordinary solids, however, are known to expand as the temperature is raised and vice versa. The evaluation of the entropy change from statistical considerations of rubberlike substances during expansion is a very difficult task, even for the case of ideal rubhers, and here I can do no more than refer to the papers by Pryor (29) and Guth (32) for some detail and further references.

With a negatively charged protein the effects are even more striking (Fig. 7). With a nonionogenic thiol in case (I)there is no dependence REACTIONS AT INTERFACES 53 on ionic strength. In the three other examples the degree of reduction of protein SH is markedly increased by reduction in ionic strength. D. 0, and the bulk thiol has been assumed 50% oxidized. Figure 8 Fig. 8. Ratio [PrSH]/[PrSS] a t the surface of proteins, in a solution containing various concentrations, e, of bulk phase thiol.

REACTIONS A T I N T E R F A C E S I N RELATION TO BIOLOGICAL PROBLEMS . By J F. DANIELLI and J . T. DAVIES. London. England CONTENTS I. Introduction .................................................. I1. Distribution of Soluble Ions a t Interfaces ......................... I11. Partition of SH Groups between Surface and Bulk Phases .......... A . Nonionogenic Thiols ...................................... B . Ionogenic Thiols ......................................... C. Effect of Variation in Ionic Strength ........................

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