期刊
EUROPEAN JOURNAL OF ORGANIC CHEMISTRY
卷 2012, 期 21, 页码 3946-3954出版社
WILEY-V C H VERLAG GMBH
DOI: 10.1002/ejoc.201200327
关键词
Amino acids; Peptides; Fluorinated substituents; Conformation analysis; Helical structures
资金
- American Chemical Society [46219-AC4]
- National Science Foundation (NSF) [CHE0957544]
- Direct For Mathematical & Physical Scien
- Division Of Chemistry [0957544] Funding Source: National Science Foundation
The design and synthesis of pentafluorosulfanyl-containing heptad amino acid sequence was described. The three-dimensional conformation of the peptide was investigated by using CYANA (combined assignment and dynamics algorithm for NMR applications) and the integrated autoassignment. This study shows that the one of the diastereomers assumed a very tight coiled conformation in [D6]DMSO where both pentafluorosulfanyl groups assumed a synclinal relationship. The propensity of the protected heptapeptide to form such a tight coil and of the pentafluorosulfanyl groups to align so uniformly is suggestive of the utility of pentafluorosulfanylated amino acids in promoting conformational control.
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