2014
DOI: 10.1016/j.jmr.2013.12.008
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Toward optimal-resolution NMR of intrinsically disordered proteins

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Cited by 30 publications
(27 citation statements)
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“…High solvent exposure leads to similar local environments for all residues, leading to collapsed spectra with overlapping peaks. Additionally, the generally lower complexity of IDPs, relative to ordered proteins, leads to additional environmental symmetry between residues and further collapse of spectra (Felli and Pierattelli 2014;Nováček et al 2014).…”
Section: Developing Improved Methods For the Study Of Idps By Nmrmentioning
confidence: 99%
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“…High solvent exposure leads to similar local environments for all residues, leading to collapsed spectra with overlapping peaks. Additionally, the generally lower complexity of IDPs, relative to ordered proteins, leads to additional environmental symmetry between residues and further collapse of spectra (Felli and Pierattelli 2014;Nováček et al 2014).…”
Section: Developing Improved Methods For the Study Of Idps By Nmrmentioning
confidence: 99%
“…Several approaches have been developed to overcome the high signal overlap of many IDPs (Nováček et al 2014). One of these approaches is sampling of spectra at a higher rate to resolve spectra overlap.…”
Section: Developing Improved Methods For the Study Of Idps By Nmrmentioning
confidence: 99%
See 2 more Smart Citations
“…Konrat offers a general review on the contributions of NMR to the study of IDPs, 58 while Novacek et al provide a review in the on the progress toward optimal-resolution NMR. 59 Felli and Pierattelli discuss 13 C based methods in the study of IDPs. 60 In the Journal of Biomolecular NMR, Pantoja-Uceda and Santoro present new 13 C-detected experiments that can correlate consecutive 13 C'-15 N groups in IDPs and that also provide recognition of glycine residues, facilitating the assignment process.…”
Section: Experimental Approaches For the Analysis Of Intrinsic Disordermentioning
confidence: 99%