SHORT COMMUNICATION Chameleon sequences in the PDB
نویسنده
چکیده
There has been recent interest in exploring the possibilities of a given amino acid sequence assuming different secondary structures in different contexts. An 11-residue segment of a synthetic protein was successfully designed that formed an α helix in one context and a β sheet in another, prompting the authors to dub it a ‘chameleon’ sequence (Minor and Kim, 1996). On a larger scale, a 56-residue protein domain was successfully converted to a different fold by changing no more than half of the residues (Dalal et al., 1997). The fact that this achievement was prompted by a challenge supplemented by a monetary prize by some of the leaders in the protein folding field (Rose and Creamer, 1994) indicates the strength of the belief that the secondary structure of a protein is essentially determined locally by the primary structure.
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تاریخ انتشار 1998