Cooperative folding units of Escherichia coli tryptophan repressor

A. Wallqvist, T. A. Lavoie, J. A. Chanatry, D. G. Covell, J. Carey

Research output: Contribution to journalArticlepeer-review

4 Scopus citations


A previously published computational procedure was used to identify cooperative folding units within tryptophan repressor. The theoretical results predict the existence of distinct stable substructures in the protein chain for the monomer and the dimer. The predictions were compared with experimental data on structure and folding of the repressor and its proteolytic fragments and show excellent agreement for the dimeric form of the protein. The results suggest that the monomer, the structure of which is currently unknown, is likely to have a structure different from the one it has within the context of the highly intertwined dimer. Application of this method to the repressor monomer represents an extension of the computations into the realm of evaluating hypothetical structures such as those produced by threading.

Original languageEnglish (US)
Pages (from-to)1619-1626
Number of pages8
JournalBiophysical Journal
Issue number3
StatePublished - Sep 1999

All Science Journal Classification (ASJC) codes

  • Biophysics


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