By C.B. Anfinsen, John T. Edsall, Frederic M. Richards, David S. Eisenberg and George Lorimer (Eds.)

Experiences present issues within the box of protein chemistry. the themes lined comprise the constitution and mechanism of heat-shock-related proteins, the function of prolylisomerases in protein folding, and the mechanism of enzymic and nonenzymic prolylcis-transisomerization.

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Refolding of RNase T 1 apparently occurs on a minor fast and two major slow pathways. This is revealed when an unfolding assay is used to determine the time course of formation of native molecules. The assay is based on the finding that the completely folded species, N , is separated from all other unfolded or partially folded molecules by a high activation barrier. Therefore only N molecules unfold slowly, whereas partially folded intermediates unfold rapidly. The folding kinetics obtained by this method are thus not affected by the formation of such intermediates.

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And Braun, W. (1991). Science 254, 953-954. PROLYL ISOMERASES: ROLE IN PROTEIN FOLDING By FRANZ X. SCHMID, LOREN2 M. MAYR, MATTHIAS MUCKE, and E. RALF SCHONBRUNNER Laboratorium fiir Biochemie, Universitlt Bayreuth, D-W-8580 Bayreuth, Germany I. Introduction . . . ....................... 11. Prolyl Isomerization A. Fast and Slow Protein Folding Reactions . . . . . . . . , . . . . B. Prolyl Peptide Bonds . . . . . . . . . . . . . . . . C. Prolyl Isomerization in Protein Folding .

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