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. 1993 Dec;2(12):2134–2145. doi: 10.1002/pro.5560021213

Origins of structural diversity within sequentially identical hexapeptides.

B I Cohen 1, S R Presnell 1, F E Cohen 1
PMCID: PMC2142335  PMID: 8298461

Abstract

Efforts to predict protein secondary structure have been hampered by the apparent structural plasticity of local amino acid sequences. Kabsch and Sander (1984, Proc. Natl. Acad. Sci. USA 81, 1075-1078) articulated this problem by demonstrating that identical pentapeptide sequences can adopt distinct structures in different proteins. With the increased size of the protein structure database and the availability of new methods to characterize structural environments, we revisit this observation of structural plasticity. Within a set of proteins with less than 50% sequence identity, 59 pairs of identical hexapeptide sequences were identified. These local structures were compared and their surrounding structural environments examined. Within a protein structural class (alpha/alpha, beta/beta, alpha/beta, alpha + beta), the structural similarity of sequentially identical hexapeptides usually is preserved. This study finds eight pairs of identical hexapeptide sequences that adopt beta-strand structure in one protein and alpha-helical structure in the other. In none of the eight cases do the members of these sequences pairs come from proteins within the same folding class. These results have implications for class dependent secondary structure prediction algorithms.

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Selected References

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