Ionic Processes in Solution - download pdf or read online

By Curney R.W. (ed.)

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The exposed and interlocked Thr-Gly p-turn appears to be a highly conserved structural motif of TIM. Thus, it is of interest to examine whether the exposed Thr-Gly p-turn is a unique structural motif of the dimeric TIM enzyme or whether it is also found in other protein structures. A protocol of related searches for primary and secondary structure information in ROPDB (ROche Protein structure Data Base)1,2 is reproduced in Figure 6. Again, relevant information is readily gathered. A number of occurrencies of Thr-Gly or Ser-Gly p-turns are uncovered in a variety of proteins and enzymes.

V. Ganin, Yu. A. F. L. Kamalov, 'Structure of macrocyc1ic phthalic acid diamides', Zh. Strukt. Khim 23:103 (1982). 18. F. K. Winkler and J. D. Dunitz, 'Medium-Ring Compounds. XXVII. Caprinolactam Hemihydrochloride', Acta Cryst. B31:286 (1975). 19. M. B. Hossain and D. van der Helm, 'Conformation and Crystal Structures of Two Cyc1oisomeric Hexapeptides: cyc1o-(L-Alanyl-Lalanylglycylglycyl-L-alanylglycyl) Monohydrate (I) and cyc1o-(LAlanyl-L-alanylglycyl-L-alanylglycylglycyl) Dihydrate (II)', J. Am.

A protocol of related searches for primary and secondary structure information in ROPDB (ROche Protein structure Data Base)1,2 is reproduced in Figure 6. Again, relevant information is readily gathered. A number of occurrencies of Thr-Gly or Ser-Gly p-turns are uncovered in a variety of proteins and enzymes. The observation that this structural motif is also found well exposed on the surface of some antibodies 14 and viral coat proteins 15 indicates interesting opportunities for further potential applications of cyclic Thr-Gly containing loop analogs.

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Ionic Processes in Solution by Curney R.W. (ed.)


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