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• W2080751500 endingPage "11" @default.
• W2080751500 startingPage "7" @default.
• W2080751500 abstract "The molecular conformation of ubiquitinated structures and the validity of the N-end rule were examined by simulating the molecular mechanics to ascertain the global energy-minimized structure. We examined the chemical linkage involved in attaching the ubiquitin carboxyl terminus to the N-terminus of three different x-hexapeptides, where x is the amino group of the acceptor peptide--either valine, arginine or glutamic acid--(x-K linkage) and to the epsilon-amino group of lysine of the acceptor hexapeptide x-glu1-his2-lys3-gly4-lys5-val6 (K-K linkage) through the formation of an isopeptide bond. Changes in conformation and molecular stability of the multi-ubiquitinated structures were determined by energy-minimization procedures using the SYBYL program developed by Tripos Associates. In the x-K linkage, the ubiquitin molecule is stretched in the beta-pleated sheets and beta-turns while the alpha-helices expand, as the molecule continues to unfold linearly. In the K-K linkage, the ubiquitin molecules have turned into a u-shaped, semi-circular alignment, contracting into a compact, folded structure." @default.
• W2080751500 created "2016-06-24" @default.
• W2080751500 creator A5072112518 @default.
• W2080751500 creator A5075009615 @default.
• W2080751500 date "1992-03-01" @default.
• W2080751500 modified "2023-09-23" @default.
• W2080751500 title "Molecular conformation of ubiquitinated structures and the implications for regulatory function" @default.
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• W2080751500 doi "https://doi.org/10.1016/0263-7855(92)80002-u" @default.
• W2080751500 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/1323999" @default.
• W2080751500 hasPublicationYear "1992" @default.
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