Proteins de novo design

Dahiyat, B.I., Mayo, S.L. De novo protein design fully automated sequence selection. Science 278 82-87,... 

B. I. Dahiyat, C. A. Sarisky, S. L. Mayo. De novo protein design towards fully automated sequence selection. J Mol Biol. 1997, 273, 789-796. 

Helical folds have dominated in the pioneering development of de novo protein design [18] and have also been the most common in the design of new catalysts [4—9, 11-14], Fig. 5.1. The robustness of the motif has been a contributing factor... 

Figure 5.1. Modelled structure of a 42-residue peptide folded into a helix-loop-helix motif and dimerized to form a four-helix bundle protein. Helices are amphiphilic with a hydrophobic and a polar face. Due to the robustness and ease of synthesis this has become a popular motif in de novo protein design.

The above results show how combining the principles of supramolecular coordination chemistry with those of de novo protein design can produce a new family of metal-peptide nanoassemblies in which metal coordination is used to promote the formation of a-helical coiled-coils having discrete molecular... 

Understanding the Biological Chemistry of Mercury Using a de novo Protein Design... 

Dahiyat, B. I., and Mayo, S. L. (1997). De novo protein design Fully automated sequence selection. Science 278(5335), 82-87. 

The molecular middle ground between nonheme di-iron enzymes and their small molecule synthetic analogues has been explored by de novo protein design. A protein can be designed to fold into a predetermined tertiary structure without patterning the sequence after any natural... 

D. T. Jones, Protein Sci., 3, 567 (1994). De Novo Protein Design Using Pairwise Potentials and a Genetic Algorithm. 

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