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• W2007486560 endingPage "968" @default.
• W2007486560 startingPage "961" @default.
• W2007486560 abstract "It is widely believed that the dominant force opposing protein folding is the entropic cost of restricting internal rotations. The energetic changes from restricting side-chain torsional motion are more complex than simply a loss of conformational entropy, however. A second force opposing protein folding arises when a side-chain in the folded state is not in its lowest-energy rotamer, giving rotameric strain. chi strain energy results from a dihedral angle being shifted from the most stable conformation of a rotamer when a protein folds. We calculated the energy of a side-chain as a function of its dihedral angles in a poly(Ala) helix. Using these energy profiles, we quantify conformational entropy, rotameric strain energy and chi strain energy for all 17 amino acid residues with side-chains in alpha-helices. We can calculate these terms for any amino acid in a helix interior in a protein, as a function of its side-chain dihedral angles, and have implemented this algorithm on a web page. The mean change in rotameric strain energy on folding is 0.42 kcal mol-1 per residue and the mean chi strain energy is 0.64 kcal mol-1 per residue. Loss of conformational entropy opposes folding by a mean of 1.1 kcal mol-1 per residue, and the mean total force opposing restricting a side-chain into a helix is 2.2 kcal mol-1. Conformational entropy estimates alone therefore greatly underestimate the forces opposing protein folding. The introduction of strain when a protein folds should not be neglected when attempting to quantify the balance of forces affecting protein stability. Consideration of rotameric strain energy may help the use of rotamer libraries in protein design and rationalise the effects of mutations where side-chain conformations change." @default.
• W2007486560 created "2016-06-24" @default.
• W2007486560 creator A5000626384 @default.
• W2007486560 creator A5005165880 @default.
• W2007486560 date "2001-01-01" @default.
• W2007486560 modified "2023-09-27" @default.
• W2007486560 title "Rotamer strain energy in protein helices - quantification of a major force opposing protein folding" @default.
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• W2007486560 doi "https://doi.org/10.1006/jmbi.2000.4339" @default.
• W2007486560 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/11162106" @default.
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