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. 1995 Jun;4(6):1167–1177. doi: 10.1002/pro.5560040615

Domains in folding of model proteins.

V I Abkevich 1, A M Gutin 1, E I Shakhnovich 1
PMCID: PMC2143143  PMID: 7549881

Abstract

By means of Monte Carlo simulation, we investigated the equilibrium between folded and unfolded states of lattice model proteins. The amino acid sequences were designed to have pronounced energy minimum target conformations of different length and shape. For short fully compact (36-mer) proteins, the all-or-none transition from the unfolded state to the native state was observed. This was not always the case for longer proteins. Among 12 designed sequences with the native structure of a fully compact 48-mer, a simple all-or-none transition was observed in only three cases. For the other nine sequences, three states of behavior-the native, denatured, and intermediate states-were found. The contiguous part of the native structure (domain) was conserved in the intermediate state, whereas the remaining part was completely unfolded and structureless. These parts melted separately from each other.

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Selected References

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