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• W2158163089 abstract "It has been suggested that Φ-values, which allow structural information about transition states (TSs) for protein folding to be obtained, are most reliably interpreted when divided into three classes (high, medium and low). High Φ-values indicate almost completely folded regions in the TS, intermediate Φ-values regions with a detectable amount of structure and low Φ-values indicate mostly unstructured regions. To explore the extent to which this classification can be used to characterise in detail the structure of TSs for protein folding, we used Φ-values divided into these classes as restraints in molecular dynamics simulations. This type of procedure is related to that used in NMR spectroscopy to define the structure of native proteins from the measurement of inter-proton distances derived from nuclear Overhauser effects. We illustrate this approach by determining the TS ensembles of five proteins and by showing that the results are similar to those obtained by using as restraints the actual numerical Φ-values measured experimentally. Our results indicate that the simultaneous consideration of a set of low-resolution Φ-values can provide sufficient information for characterising the architecture of a TS for folding of a protein." @default.
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• W2158163089 date "2008-01-18" @default.
• W2158163089 modified "2023-09-24" @default.
• W2158163089 title "Characterisation of transition state structures for protein folding using 'high', 'medium' and 'low' -values" @default.
• W2158163089 cites W1530704185 @default.
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• W2158163089 doi "https://doi.org/10.1093/protein/gzm092" @default.
• W2158163089 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/2397543" @default.
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