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 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.

Show description

Read or Download Accessory Folding Proteins PDF

Similar chemistry books

Chemie didaktik. Diagnose und Korrektur von Schulervorstellungen

Unterrichtsplaner gingen lange davon aus, dass Schüler kaum eigene Vorstellungen in den Unterricht mitbringen. Fachdidaktische Erhebungen zeigen allerdings, dass Kinder und Jugendliche sehr wohl eigene Ideen zu Natur und Alltag haben. Chemiedidaktiker ermöglichen erfolgreiches Lernen, indem sie diese diagnostizieren.

The Chemistry of Mood, Motivation, and Memory: The proceedings of an interdisciplinary conference on the Chemistry of Mood, Motivation, and Memory held at the University of California, San Francisco, in October 1971

This quantity relies on shows at an interdisciplinary convention at the Chemistry of temper, Motivation and reminiscence which was once held on the college of California, San Francisco in October, 1971. The convention used to be backed and supported by way of the department of constant schooling in future health Sciences.

Additional info for Accessory Folding Proteins

Sample text

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.

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. Quinn, D. , and Sutton, L. D. (1991). In “Enzyme Mechanism from Isotope Effects” (P. F. ), pp. 73-126. CRC Press, Boston. , and Wolfenden, R. (1988). Biochemistry 27, 4538-4541. Ritchie, C. , and Sager, W. F. (1964).

Download PDF sample

Rated 4.76 of 5 – based on 30 votes