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- W963420662 abstract "Publisher Summary This chapter summarizes developments in heteronuclear 3D and 4D NMR studies designed to extend the NMR methodology to medium-sized proteins in the range 15-30 kDa. The underlying principle of this approach consists of extending the dimensionality of the spectra to obtain dramatic improvements in spectral resolution while simultaneously exploiting large heteronuclear couplings to circumvent problems associated with larger line widths. A key feature of all the experiments is that they do not result in any increase in the number of observed cross-peaks relative to the 2D counterparts. Hence, the improvement in resolution is achieved without raising the spectral complexity, rendering data interpretation straightforward. Thus, for example, in 4D heteronuclear-edited NOESY spectra, the NOE interactions between proton pairs are labeled not only by the H chemical shifts, but also by the corresponding chemical shifts of their directly bonded heteronuclei in four orthogonal axes of the spectrum. Subsequently, a number of other medium-sized protein structures have been determined using these methods, including those of interleukin a complex of calmodulin with a target peptide, and a complex of cyclophilin and cyclosporin A." @default.
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- W963420662 title "[11] Multidimensional heteronuclear nuclear magnetic resonance of proteins" @default.
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- W963420662 doi "https://doi.org/10.1016/s0076-6879(94)39013-4" @default.
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