Download A table of anti-logarithms to seven places and Gauss by Herschell E Filipowski PDF

By Herschell E Filipowski

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The refolding experiments were carried out as described in the legend to Fig. 4. From Schonbrunner et al. (1991). 42 FRANZ X. SCHMID E T AL. D. Dependence of Catalysis on Presence of Prolines The name prolyl isomerase implies that this enzyme acts by catalyzing the isomerization of prolyl peptide bonds. This has been shown conclusively for the short synthetic peptide glutaryl-Ala-Ala-Pro-Phe-4-nitroanilide. , 1984). Only proline-containing peptides were able to compete with this substrate in the assay; proline free peptides or protein fragments had no effect.

According to Scheme 11, protein folding and reisomerization of prolyl peptide bonds are interrelated processes in the refolding of RNase T1. Under strongly native conditions intermediates with nativelike secondary structure are formed very rapidly and they can tolerate the presence of nonnative proline isomers. Their stability, however, is lowered by these incorrect isomers, and they are not populated under marginally native conditions. Pro39 and Pro55 of RNase T 1 could thus be classified as “type 11” prolines (cf.

Introduction . . . ....................... 11. Prolyl Isomerization A. Fast and Slow Protein Folding Reactions . . . . . . . . , . . . . B. Prolyl Peptide Bonds . . . . . . . . . . . . . . . . C. Prolyl Isomerization in Protein Folding . . 111. Prolyl Isomerases A. B. C. D. Discovery of P Three-Dimensional Structure of Cyclophilin Cyclophilin Family . . . . . . . . . . . . . . . . . . . . . . Catalysis of Slow-Folding Steps IV. V. VI. B. Dependence on Substrate Concentration of Folding Catalysis C .

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