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• W2073876360 abstract "What governs the balance between connectivity and topology in regulating the mechanism of protein folding? We use circular permutation to vary the order of the helices in the all-α Greek key protein FADD (Fas-associated death domain) to investigate this question. Unlike all-β Greek key proteins, where changes in the order of secondary structure cause a shift in the folding nucleus, the position of the nucleus in FADD is unchanged, even when permutation reduces the complexity significantly. We suggest that this is because local helical contacts are so dominant that permutation has little effect on the entropic cost of forming the folding nucleus whereas, in all-β Greek key proteins, all interactions in the nucleus are long range. Thus, the type of secondary structure modulates the sensitivity of proteins to changes in connectivity." @default.
• W2073876360 created "2016-06-24" @default.
• W2073876360 creator A5020633703 @default.
• W2073876360 creator A5054817549 @default.
• W2073876360 creator A5061727643 @default.
• W2073876360 date "2015-06-01" @default.
• W2073876360 modified "2023-10-18" @default.
• W2073876360 title "The Response of Greek Key Proteins to Changes in Connectivity Depends on the Nature of Their Secondary Structure" @default.
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• W2073876360 doi "https://doi.org/10.1016/j.jmb.2015.03.020" @default.
• W2073876360 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/4451459" @default.
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• W2073876360 hasPublicationYear "2015" @default.
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