Accessory Folding Proteins by C.B. Anfinsen, John T. Edsall, Frederic M. Richards, David

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

Studies present themes within the box of protein chemistry. the topics lined contain 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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An immunoglobulin fragment with a single czs-prolyl peptide bond displays 20% U, after unfolding (Goto and Hamaguchi, 1982). Brandts et al. (1977) and Lin and Brandts (1978) have studied the refolding of three homologous carp parvalbumins. Two of them contain one proline residue, and they show a small, slow refolding reaction. Such a reaction is not found in the folding of the third parvalbumin variant that lacks proline. 2. T h e U, 2 Us reactions in unfolded proteins have properties that are characteristic of prolyl peptide bond isomerizations in small peptides.

Org. Chem. 55,4984-4986. Berarek, V. (1973). Actu Chin. Pulacki. , Fac. Rerum Nut. 41, 11 1-1 15. , and Meiboom, S. J. Am. Chem. SOC. 81,62-67. Brandts, J. , and Lin, L. N. (1977). Proc. Natl. Acad. Sci. A. 74, 7312-7317. Challis, B. , and Challis, J. A. (1979). “Nitrogen Compounds, Carboxylic Acids, Phosphorous Compounds,” pp. 957- 1067. Pergamon, Oxford. Cheng, H. , and Bovey, F. A. (1977). Biopolymers 16, 1465-1472. Cleland, W. W. (1975). Adv. Enzymol. 45, 273-387. Cleland, W. W. (1982). In “Methods in Enzymology” (D.

Folding and unfolding reactions can be studied in the presence and in the absence of the two disulfide bonds. Furthermore, an interesting interrelationship between the two slow events, prolyl isomerization and formation of disulfide bonds, is observed in the oxidative folding of reduced RNase T1. A. , 1989). The structure is shown schematically in Fig. 3. Two disulfide bonds form a small (2-10) and a large (6-103) covalently linked loop. RNase T 1 contains four prolyl peptide bonds; two are trans (Trp59Pro60 and Ser72-Pro73) and the other two are cis (Tyr38-Pro39 and N cis-Pro39 FIG.

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