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• W1498503622 endingPage "1177" @default.
• W1498503622 startingPage "1167" @default.
• W1498503622 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." @default.
• W1498503622 created "2016-06-24" @default.
• W1498503622 creator A5071147112 @default.
• W1498503622 creator A5082765817 @default.
• W1498503622 creator A5089469355 @default.
• W1498503622 date "1995-06-01" @default.
• W1498503622 modified "2023-09-28" @default.
• W1498503622 title "Domains in folding of model proteins" @default.
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• W1498503622 doi "https://doi.org/10.1002/pro.5560040615" @default.
• W1498503622 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/2143143" @default.
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• W1498503622 hasPublicationYear "1995" @default.
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