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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Chem. 76, 853-855. Lumry, R. (1986). I n “The Fluctuating Enzyme” (G. R. ), p. 6. Wiley, New York. , and Rajender, S. (1970). Eiopolymers 9, 1125-1227. Martin, R. B. J . Chem. , Chem. Commun. pp. 793-794. McCall, J. M. J. Med. Chem. 18, 549-552. Michnick, S. , Rosen, M. , Wandless, T. , and Schreiber, S. L. (1991). Science 252, 836-839. 24 ROSS L. STEIN Moore, J. , Peattie, D. , Fitzgibbon, M. , and Thompson, J. A. Nature (London) 351,248-250. Nemethy, G . (1967). Angew. , Int. Ed. Engl. 6 , 195-206.

Cis cis trans isornerization of' a prolyl peptide bond. A plausible molecular explanation for this phenomenon was provided by the proline hypothesis of Brandts et al. (1975). They suggested that the fast- and slow-folding molecules differ in the cis-trans isomeric state of one or more Xaa-Pro peptide bonds (cf. Fig. 1). B . Prolyl Peptide Bonds Peptide bonds are planar and can be either in the trans or in the cis conformation with respect to the two successive C, positions. These conformations are equivalent to dihedral angles w of 180" and 0", respectively.

And Grunwald, E. (1963). “Rates and Equilibrium in Organic Reactions,” pp. 321, 325, 358. Wiley, New York. , and Brandts, J. F. (1983). Biochemistry 22, 553-559. , Albers, M. , Chen, C. , Schreiber, S. , and Wakh, C. T. (1990). Proc. Natl. Acad. Sci. A. 87, 2304-2308. Love, A. , Alger, T. , and Olsen, R. K. J. Phys. Chem. 76, 853-855. Lumry, R. (1986). I n “The Fluctuating Enzyme” (G. R. ), p. 6. Wiley, New York. , and Rajender, S. (1970). Eiopolymers 9, 1125-1227. Martin, R. B. J . Chem. , Chem.

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