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• W2074146738 endingPage "649" @default.
• W2074146738 startingPage "642" @default.
• W2074146738 abstract "Chain entanglements provide a simple and global measure of folding in a macromolecule. The complexity of these entanglements can be expressed by the pattern of projected bond-bond crossings, or overcrossings, associated with the molecular backbone. In this work, we use this approach to characterize quantitatively the range of tertiary folds observed in proteins with a given chain length. To discriminate among folding features, we use two shape descriptors derived from the probability distribution of overcrossings: the mean overcrossing number, N, and the most probable overcrossing number, N*. The values of N and N* relate to the content of secondary structure in a protein as well as its global three-dimensional organization. We propose a measure of folding diversity based on the properties of these descriptors. In addition, we discuss the application of our method to study how tertiary folds evolve during protein dynamics." @default.
• W2074146738 created "2016-06-24" @default.
• W2074146738 creator A5009658010 @default.
• W2074146738 creator A5040615574 @default.
• W2074146738 date "1999-05-21" @default.
• W2074146738 modified "2023-10-09" @default.
• W2074146738 title "Characterization of Fold Diversity among Proteins with the Same Number of Amino Acid Residues" @default.
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• W2074146738 doi "https://doi.org/10.1021/ci990323i" @default.
• W2074146738 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/10443026" @default.
• W2074146738 hasPublicationYear "1999" @default.
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