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• W1188919047 startingPage "363" @default.
• W1188919047 abstract "This chapter describes chemical shift standards and pointing out some of the necessary corrections and experimental recommendations that need to be followed so that the NMR community can exploit chemical shift information to the fullest. Chemical shift analysis holds much promise for the field of protein NMR. There are two very different chemical shift standards are being used has led to the appearance of several very different tables for random coil 13C chemical shifts, which has already caused a good deal of confusion within the NMR community. In particular case, chemical shift analysis was applied to a small, flexible peptide to both localize and quantify helix content as a function of TFE concentration. By monitoring the TFE-induced displacement of assigned a-13C resonances, the extent of the relative chemical shift change could be correlated with the intensity of the helical CD signal. These chemical shift plots are reported to provide qualitative details on the flexibility of the molecule and the presence of possible nonnative conformers." @default.
• W1188919047 created "2016-06-24" @default.
• W1188919047 creator A5003573061 @default.
• W1188919047 creator A5067477469 @default.
• W1188919047 date "1994-01-01" @default.
• W1188919047 modified "2023-10-16" @default.
• W1188919047 title "[12] Chemical shifts as a tool for structure determination" @default.
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• W1188919047 doi "https://doi.org/10.1016/s0076-6879(94)39014-2" @default.
• W1188919047 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/7830591" @default.
• W1188919047 hasPublicationYear "1994" @default.
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