By C.B. Anfinsen, John T. Edsall, Frederic M. Richards, David S. Eisenberg and George Lorimer (Eds.)
Studies present subject matters within the box of protein chemistry. the topics coated contain the constitution and mechanism of heat-shock-related proteins, the position of prolylisomerases in protein folding, and the mechanism of enzymic and nonenzymic prolylcis-transisomerization.
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SCHMID ET AL. , 1984) additional members of the cyclophilin family were detected in many cells and tissues. , 1989; Liu and Walsh, 1990). , 199 1). 4% of the total cellular protein. The amino acid sequences of the cyclophilins remained highly conserved during evolution. This holds in particular for the proteins from eukaryotes. , 1987). The homology between the mammalian cyclophilins and the cytosolic PPI from E . , 1991). The PPIs from porcine kidney and E . cola cytoplasm were used in most of the work on the function of prolyl isomerases as catalysts of protein folding that will be discussed herein.
The trans state is strongly favored for peptide bonds that d o not involve proline residues. , 1975,Jorgensen and Gao, 1988). , 1990; MacArthur and Thornton, 1991). Unlike other peptide bonds, those between proline and its preceding amino acid (Xaa-Pro bonds, Fig. 1) typically exist as a mixture of cis and trans isomers in solution, unless structural constraints, such as in folded proteins, stabilize one of the two isomers. T h e trans isomer is usually favored slightly over the cis isomer in the absence of ordered structure and in short linear peptides.
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