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- W2023290399 endingPage "579" @default.
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- W2023290399 abstract "Abstract: 2,2,6,6-Tetramethylpiperidine-1-oxyl-4-amino-4-carboxylic acid (TOAC) is a topographically and conformationally restricted, nitroxide containing, Cα-tetrasubstituted α-amino acid. Here, we describe the molecular and crystal structures, as determined by X-ray diffraction analyses, of a TOAC terminally protected derivative, the cyclic dipeptide c(TOAC)2·1,1,1,3,3,3-hexafluoropropan-2-ol (HFIP) solvate, and five TOAC-containing, terminally protected, linear peptides ranging in length from tetra- to hepta-peptides. Incipient and fully developed, regular or distorted 310-helical structures are formed by the linear peptides. A detailed discussion on the average geometry and preferred conformation for the TOAC piperidine ring is also reported. The X-ray diffraction structure of an intramolecularly cyclized side product resulting from a C-activated TOAC residue has also been determined." @default.
- W2023290399 created "2016-06-24" @default.
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- W2023290399 date "2005-06-01" @default.
- W2023290399 modified "2023-09-25" @default.
- W2023290399 title "A topographically and conformationally constrained, spin-labeled, alpha-amino acid: crystallographic characterization in peptides*" @default.
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- W2023290399 doi "https://doi.org/10.1111/j.1399-3011.2005.00258.x" @default.
- W2023290399 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/15885116" @default.
- W2023290399 hasPublicationYear "2005" @default.
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